产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
展开/折叠
Villin 2 ezrin; CVIL; CVL; Cytovillin 2; Cytovillin; DKFZp762H157; Epididymis secretory protein Li 105; EZR; EZRI_HUMAN; Ezrin; FLJ26216; HEL S 105; MGC1584; p81; VIL 2; VIL2; Villin 2 (ezrin); Villin 2; Villin-2; Villin2; Epididymis luminal protein 70; HEL70; Membrane organizing extension spike protein; Membrane-organizing extension spike protein; MOES_HUMAN; Moesin; Moesin/anaplastic lymphoma kinase fusion protein; Msn; MSN/ALK fusion; CB567; CG12537; DFNB24; ESP10; Hh-induced MATH and BTB domain-containing protein; HIB; Moesin-B; Protein roadkill; RADI_HUMAN; Radixin; RDX;
抗原和靶标
A synthesized peptide derived from human Moesin/Ezrin/Radixin.
Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied.
P26038 MOES_HUMAN:In all tissues and cultured cells studied.
- P15311 EZRI_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL
- P26038 MOES_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
- P35241 RADI_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLKQIEEQTIKAQKELEEQTRKALELDQERKRAKEEAERLEKERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEHDENNAEASAELSNEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM
翻译修饰 - P15311/P26038/P35241 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K3 | Ubiquitination | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
T57 | Phosphorylation | Uniprot | |
K60 | Acetylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
S66 | Phosphorylation | P17612 (PRKACA) | Uniprot |
K72 | Ubiquitination | Uniprot | |
K79 | Acetylation | Uniprot | |
K79 | Ubiquitination | Uniprot | |
K83 | Ubiquitination | Uniprot | |
K107 | Ubiquitination | Uniprot | |
S112 | Phosphorylation | Uniprot | |
Y116 | Phosphorylation | Uniprot | |
Y137 | Phosphorylation | Uniprot | |
K139 | Acetylation | Uniprot | |
K139 | Ubiquitination | Uniprot | |
K143 | Ubiquitination | Uniprot | |
S144 | Phosphorylation | Uniprot | |
Y146 | Phosphorylation | P00533 (EGFR) , P16591 (FER) , P12931 (SRC) , P06239 (LCK) | Uniprot |
S149 | Phosphorylation | Uniprot | |
K162 | Ubiquitination | Uniprot | |
R171 | Methylation | Uniprot | |
K184 | Acetylation | Uniprot | |
K184 | Ubiquitination | Uniprot | |
Y191 | Phosphorylation | Uniprot | |
Y201 | Phosphorylation | Uniprot | |
Y205 | Phosphorylation | Uniprot | |
K209 | Ubiquitination | Uniprot | |
K211 | Ubiquitination | Uniprot | |
K230 | Sumoylation | Uniprot | |
K230 | Ubiquitination | Uniprot | |
K233 | Sumoylation | Uniprot | |
K233 | Ubiquitination | Uniprot | |
T235 | Phosphorylation | Q00535 (CDK5) | Uniprot |
K237 | Ubiquitination | Uniprot | |
S243 | Phosphorylation | Uniprot | |
S249 | Phosphorylation | Uniprot | |
K253 | Acetylation | Uniprot | |
K253 | Ubiquitination | Uniprot | |
K254 | Ubiquitination | Uniprot | |
K258 | Acetylation | Uniprot | |
K258 | Ubiquitination | Uniprot | |
K262 | Acetylation | Uniprot | |
K262 | Sumoylation | Uniprot | |
K262 | Ubiquitination | Uniprot | |
K263 | Acetylation | Uniprot | |
K263 | Ubiquitination | Uniprot | |
Y270 | Phosphorylation | Uniprot | |
R273 | Methylation | Uniprot | |
Y291 | Phosphorylation | Uniprot | |
K296 | Ubiquitination | Uniprot | |
T299 | Phosphorylation | Uniprot | |
K306 | Methylation | Uniprot | |
K306 | Ubiquitination | Uniprot | |
T332 | Phosphorylation | Uniprot | |
K337 | Ubiquitination | Uniprot | |
K344 | Ubiquitination | Uniprot | |
Y354 | Phosphorylation | P16591 (FER) , P00533 (EGFR) | Uniprot |
K357 | Sumoylation | Uniprot | |
K357 | Ubiquitination | Uniprot | |
S366 | Phosphorylation | Uniprot | |
R393 | Methylation | Uniprot | |
K412 | Acetylation | Uniprot | |
K412 | Ubiquitination | Uniprot | |
S413 | Phosphorylation | Uniprot | |
Y424 | Phosphorylation | Uniprot | |
T425 | Phosphorylation | Uniprot | |
K427 | Ubiquitination | Uniprot | |
R435 | Methylation | Uniprot | |
K438 | Ubiquitination | Uniprot | |
K450 | Ubiquitination | Uniprot | |
K458 | Ubiquitination | Uniprot | |
T468 | Phosphorylation | Uniprot | |
Y478 | Phosphorylation | P12931 (SRC) , P16591 (FER) | Uniprot |
S482 | Phosphorylation | Uniprot | |
Y483 | Phosphorylation | Uniprot | |
S488 | Phosphorylation | Uniprot | |
T497 | Phosphorylation | Uniprot | |
Y499 | Phosphorylation | Uniprot | |
K523 | Ubiquitination | Uniprot | |
S535 | Phosphorylation | Uniprot | |
S536 | Phosphorylation | Uniprot | |
S539 | Phosphorylation | Uniprot | |
T548 | Phosphorylation | Uniprot | |
Y565 | Phosphorylation | Uniprot | |
T567 | Phosphorylation | P17252 (PRKCA) , Q5S007 (LRRK2) , P41279 (MAP3K8) , O94804 (STK10) , O95819 (MAP4K4) , P25098 (GRK2) , P31751 (AKT2) , Q13464 (ROCK1) , Q04759 (PRKCQ) , Q9P289 (STK26) , P41743 (PRKCI) , O75116 (ROCK2) | Uniprot |
T576 | Phosphorylation | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K3 | Ubiquitination | Uniprot | |
K35 | Ubiquitination | Uniprot | |
Y55 | Phosphorylation | Uniprot | |
T66 | Phosphorylation | Uniprot | |
K72 | Ubiquitination | Uniprot | |
K79 | Acetylation | Uniprot | |
K79 | Ubiquitination | Uniprot | |
K83 | Ubiquitination | Uniprot | |
Y128 | Phosphorylation | Uniprot | |
Y134 | Phosphorylation | Uniprot | |
Y137 | Phosphorylation | Uniprot | |
K139 | Ubiquitination | Uniprot | |
K143 | Ubiquitination | Uniprot | |
R151 | Methylation | Uniprot | |
K162 | Ubiquitination | Uniprot | |
K165 | Ubiquitination | Uniprot | |
K209 | Ubiquitination | Uniprot | |
K233 | Ubiquitination | Uniprot | |
K237 | Ubiquitination | Uniprot | |
S243 | Phosphorylation | Uniprot | |
S249 | Phosphorylation | Uniprot | |
K253 | Acetylation | Uniprot | |
K253 | Ubiquitination | Uniprot | |
K254 | Ubiquitination | Uniprot | |
K258 | Acetylation | Uniprot | |
K258 | Ubiquitination | Uniprot | |
K262 | Acetylation | Uniprot | |
K262 | Sumoylation | Uniprot | |
K262 | Ubiquitination | Uniprot | |
K263 | Acetylation | Uniprot | |
K263 | Ubiquitination | Uniprot | |
Y270 | Phosphorylation | Uniprot | |
R273 | Methylation | Uniprot | |
Y291 | Phosphorylation | Uniprot | |
K296 | Ubiquitination | Uniprot | |
T299 | Phosphorylation | Uniprot | |
K306 | Methylation | Uniprot | |
K306 | Ubiquitination | Uniprot | |
K335 | Ubiquitination | Uniprot | |
K344 | Acetylation | Uniprot | |
K344 | Ubiquitination | Uniprot | |
K352 | Ubiquitination | Uniprot | |
K360 | Ubiquitination | Uniprot | |
T369 | Phosphorylation | Uniprot | |
K400 | Ubiquitination | Uniprot | |
K405 | Ubiquitination | Uniprot | |
K427 | Ubiquitination | Uniprot | |
K435 | Ubiquitination | Uniprot | |
K448 | Ubiquitination | Uniprot | |
K526 | Ubiquitination | Uniprot | |
S533 | Phosphorylation | Uniprot | |
T542 | Phosphorylation | Uniprot | |
K544 | Ubiquitination | Uniprot | |
T545 | Phosphorylation | Uniprot | |
K556 | Acetylation | Uniprot | |
K556 | Ubiquitination | Uniprot | |
Y562 | Phosphorylation | Uniprot | |
T564 | Phosphorylation | O94804 (STK10) , P41279 (MAP3K8) , Q04759 (PRKCQ) , P25098 (GRK2) , O95819 (MAP4K4) , O75116 (ROCK2) , Q5S007 (LRRK2) , Q13464 (ROCK1) | Uniprot |
T573 | Phosphorylation | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K3 | Ubiquitination | Uniprot | |
T4 | Phosphorylation | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S56 | Phosphorylation | Uniprot | |
T57 | Phosphorylation | Uniprot | |
K60 | Acetylation | Uniprot | |
K64 | Acetylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
T66 | Phosphorylation | P34947 (GRK5) | Uniprot |
R71 | Methylation | Uniprot | |
K72 | Ubiquitination | Uniprot | |
S74 | Phosphorylation | Uniprot | |
K79 | Acetylation | Uniprot | |
K79 | Ubiquitination | Uniprot | |
K83 | Acetylation | Uniprot | |
K83 | Ubiquitination | Uniprot | |
T98 | Phosphorylation | Uniprot | |
K107 | Ubiquitination | Uniprot | |
Y116 | Phosphorylation | Uniprot | |
S127 | Phosphorylation | Uniprot | |
S132 | Phosphorylation | Uniprot | |
K133 | Acetylation | Uniprot | |
K139 | Acetylation | Uniprot | |
K139 | Ubiquitination | Uniprot | |
K143 | Ubiquitination | Uniprot | |
S144 | Phosphorylation | Uniprot | |
Y146 | Phosphorylation | Uniprot | |
K151 | Acetylation | Uniprot | |
K151 | Ubiquitination | Uniprot | |
K162 | Acetylation | Uniprot | |
K162 | Ubiquitination | Uniprot | |
K165 | Acetylation | Uniprot | |
K165 | Ubiquitination | Uniprot | |
Y191 | Phosphorylation | Uniprot | |
Y205 | Phosphorylation | Uniprot | |
S207 | Phosphorylation | Uniprot | |
K209 | Ubiquitination | Uniprot | |
K211 | Ubiquitination | Uniprot | |
K212 | Ubiquitination | Uniprot | |
Y228 | Phosphorylation | Uniprot | |
K237 | Ubiquitination | Uniprot | |
S243 | Phosphorylation | Uniprot | |
S249 | Phosphorylation | Uniprot | |
K253 | Acetylation | Uniprot | |
K253 | Ubiquitination | Uniprot | |
K254 | Ubiquitination | Uniprot | |
K258 | Acetylation | Uniprot | |
K258 | Ubiquitination | Uniprot | |
K262 | Acetylation | Uniprot | |
K262 | Sumoylation | Uniprot | |
K262 | Ubiquitination | Uniprot | |
K263 | Acetylation | Uniprot | |
K263 | Ubiquitination | Uniprot | |
Y270 | Phosphorylation | Uniprot | |
R273 | Methylation | Uniprot | |
Y291 | Phosphorylation | Uniprot | |
K296 | Ubiquitination | Uniprot | |
T299 | Phosphorylation | Uniprot | |
K306 | Methylation | Uniprot | |
K306 | Ubiquitination | Uniprot | |
K327 | Acetylation | Uniprot | |
K344 | Acetylation | Uniprot | |
K344 | Ubiquitination | Uniprot | |
K352 | Ubiquitination | Uniprot | |
K360 | Ubiquitination | Uniprot | |
K380 | Ubiquitination | Uniprot | |
S384 | Phosphorylation | Uniprot | |
K388 | Acetylation | Uniprot | |
K388 | Ubiquitination | Uniprot | |
K391 | Ubiquitination | Uniprot | |
K400 | Acetylation | Uniprot | |
K400 | Ubiquitination | Uniprot | |
S407 | Phosphorylation | Uniprot | |
K412 | Ubiquitination | Uniprot | |
T413 | Phosphorylation | Uniprot | |
T425 | Phosphorylation | Uniprot | |
S429 | Phosphorylation | Uniprot | |
S440 | Phosphorylation | Uniprot | |
K448 | Ubiquitination | Uniprot | |
K458 | Ubiquitination | Uniprot | |
K464 | Ubiquitination | Uniprot | |
T465 | Phosphorylation | Uniprot | |
S468 | Phosphorylation | Uniprot | |
T469 | Phosphorylation | Uniprot | |
S491 | Phosphorylation | Uniprot | |
S504 | Phosphorylation | Uniprot | |
K520 | Ubiquitination | Uniprot | |
K523 | Ubiquitination | Uniprot | |
T526 | Phosphorylation | Uniprot | |
S527 | Phosphorylation | Uniprot | |
S536 | Phosphorylation | Uniprot | |
K537 | Ubiquitination | Uniprot | |
K538 | Ubiquitination | Uniprot | |
Y556 | Phosphorylation | Uniprot | |
T558 | Phosphorylation | O95819 (MAP4K4) , Q5VT25 (CDC42BPA) , P41279 (MAP3K8) , Q04759 (PRKCQ) , O75116 (ROCK2) , Q5S007 (LRRK2) , P25098 (GRK2) , P17612 (PRKACA) , Q13464 (ROCK1) , Q9Y5S2 (CDC42BPB) , O94804 (STK10) | Uniprot |
T567 | Phosphorylation | Uniprot | |
S576 | Phosphorylation | Uniprot |
研究背景
Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.
Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity).
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.
Apical cell membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection. Cell projection>Microvillus membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection>Ruffle membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cell cortex. Cytoplasm>Cytoskeleton. Cell projection>Microvillus.
Note: Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side).
Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied.
Interacts with MPP5 and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2 (By similarity). Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity). Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition. Interacts with SPN, CD44 and ICAM2 (By similarity).
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement. These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction. The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs. Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation.
Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.
Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cytoskeleton. Apical cell membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection>Microvillus membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection>Microvillus.
Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts.
In all tissues and cultured cells studied.
In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with SLC9A3R1. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; these interaction mediate the activation of SYK by SELPLG. Interacts with PDPN (via cytoplasmic domain); this interaction activates RHOA and promotes epithelial-mesenchymal transition. Interacts with SPN/CD43. Interacts with CD44. Interacts with ICAM2 (By similarity). Interacts with ICAM3 (via C-terminus). Interacts with PDZD8. Interacts with F-actin. Interacts with CD46. Interacts with PTPN6 (By similarity).
(Microbial infection) Interacts with HIV-1 envelope protein gp120.
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.
Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity).
Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cytoskeleton. Cleavage furrow. Cell projection>Microvillus.
Note: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.
Binds SLC9A3R1. Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain). Interacts with SPN and CD44 (By similarity).
The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN (By similarity).
研究领域
· Cellular Processes > Cellular community - eukaryotes > Tight junction. (View pathway)
· Cellular Processes > Cell motility > Regulation of actin cytoskeleton. (View pathway)
· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.
· Human Diseases > Infectious diseases: Viral > Measles.
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
· Organismal Systems > Immune system > Leukocyte transendothelial migration. (View pathway)
· Organismal Systems > Digestive system > Gastric acid secretion.
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