MOES_BOVIN
ID MOES_BOVIN Reviewed; 577 AA.
AC Q2HJ49;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Moesin {ECO:0000250|UniProtKB:P26038};
DE AltName: Full=Membrane-organizing extension spike protein;
GN Name=MSN {ECO:0000250|UniProtKB:P26038};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the
CC actin cytoskeleton to the plasma membrane and thereby regulates the
CC structure and function of specific domains of the cell cortex. Tethers
CC actin filaments by oscillating between a resting and an activated state
CC providing transient interactions between moesin and the actin
CC cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin
CC is activated leading to interaction with F-actin and cytoskeletal
CC rearrangement. These rearrangements regulate many cellular processes,
CC including cell shape determination, membrane transport, and signal
CC transduction. The role of moesin is particularly important in immunity
CC acting on both T and B-cells homeostasis and self-tolerance, regulating
CC lymphocyte egress from lymphoid organs (By similarity). Modulates
CC phagolysosomal biogenesis in macrophages (By similarity). Participates
CC also in immunologic synapse formation (By similarity).
CC {ECO:0000250|UniProtKB:P26038, ECO:0000250|UniProtKB:P26041}.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding.
CC {ECO:0000250|UniProtKB:P26038}.
CC -!- SUBUNIT: In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC is disrupted upon TCR activation. Interacts with SLC9A3R1. Interacts
CC with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK;
CC these interaction mediate the activation of SYK by SELPLG. Interacts
CC with PDPN (via cytoplasmic domain); this interaction activates RHOA and
CC promotes epithelial-mesenchymal transition. Interacts with SPN/CD43
CC cytoplasmic tail (By similarity). Interacts with CD44 (By similarity).
CC Interacts with ICAM2 (By similarity). Interacts with ICAM3 (via C-
CC terminus). Interacts with PDZD8. Interacts with F-actin. Interacts with
CC CD46 (By similarity). Interacts with PTPN6 (By similarity).
CC {ECO:0000250|UniProtKB:P26038, ECO:0000250|UniProtKB:P26041}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26038};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P26041}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P26041}. Note=Phosphorylated form is enriched in
CC microvilli-like structures at apical membrane. Increased cell membrane
CC localization of both phosphorylated and non-phosphorylated forms seen
CC after thrombin treatment (By similarity). Localizes at the uropods of T
CC lymphoblasts (By similarity). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000250|UniProtKB:P26041}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P26038}.
CC -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC microvilli-like structures. Phosphorylation by ROCK2 suppresses the
CC head-to-tail association of the N-terminal and C-terminal halves
CC resulting in an opened conformation which is capable of actin and
CC membrane-binding. Phosphorylation on Thr-558 by STK10 negatively
CC regulates lymphocyte migration and polarization (By similarity).
CC {ECO:0000250}.
CC -!- PTM: S-nitrosylation of Cys-117 is induced by interferon-gamma and
CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating
CC the iNOS-S100A8/9 transnitrosylase complex.
CC {ECO:0000250|UniProtKB:P26038}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC113313; AAI13314.1; -; mRNA.
DR RefSeq; NP_001039942.1; NM_001046477.1.
DR AlphaFoldDB; Q2HJ49; -.
DR SMR; Q2HJ49; -.
DR STRING; 9913.ENSBTAP00000017503; -.
DR PaxDb; Q2HJ49; -.
DR PeptideAtlas; Q2HJ49; -.
DR PRIDE; Q2HJ49; -.
DR Ensembl; ENSBTAT00000017503; ENSBTAP00000017503; ENSBTAG00000003418.
DR GeneID; 540426; -.
DR KEGG; bta:540426; -.
DR CTD; 4478; -.
DR VEuPathDB; HostDB:ENSBTAG00000003418; -.
DR VGNC; VGNC:31703; MSN.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_003623_6_2_1; -.
DR InParanoid; Q2HJ49; -.
DR OMA; WADHKNT; -.
DR OrthoDB; 627741at2759; -.
DR TreeFam; TF313935; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000003418; Expressed in monocyte and 103 other tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
DR GO; GO:0001931; C:uropod; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0022612; P:gland morphogenesis; IEA:Ensembl.
DR GO; GO:0001771; P:immunological synapse formation; ISS:UniProtKB.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:2000401; P:regulation of lymphocyte migration; IEA:Ensembl.
DR GO; GO:1902115; P:regulation of organelle assembly; IBA:GO_Central.
DR GO; GO:0070489; P:T cell aggregation; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; S-nitrosylation.
FT CHAIN 1..577
FT /note="Moesin"
FT /id="PRO_0000254651"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 375..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..120
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT COMPBIAS 375..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26043"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 117
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26041"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 558
FT /note="Phosphothreonine; by ROCK2 and STK10"
FT /evidence="ECO:0000250|UniProtKB:P26038"
SQ SEQUENCE 577 AA; 67975 MW; F865AA486532F8EE CRC64;
MPKTINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EIWFFGLQYQ DTKGFFTWLK
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEDI LNDDIYCPPE
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD RLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQMER ALLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASQDQ KKTQEQLALE
MAELTARISQ LEMARQKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEQ
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
