MOES_PIG
ID MOES_PIG Reviewed; 577 AA.
AC P26042;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Moesin {ECO:0000250|UniProtKB:P26038};
DE AltName: Full=Membrane-organizing extension spike protein;
GN Name=MSN {ECO:0000250|UniProtKB:P26038};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8268231; DOI=10.1016/0167-4781(93)90018-9;
RA Lankes W.T., Schwartz-Albiez R., Furthmayr H.;
RT "Cloning and sequencing of porcine moesin and radixin cDNA and
RT identification of highly conserved domains.";
RL Biochim. Biophys. Acta 1216:479-482(1993).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. Plays a role in regulating the
CC proliferation, migration, and adhesion of human lymphoid cells and
CC participates in immunologic synapse formation.
CC {ECO:0000250|UniProtKB:P26038}.
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. {ECO:0000250}.
CC -!- SUBUNIT: Binds SLC9A3R1. In resting T-cells, part of a PAG1-SLC9A3R1-
CC MSN complex which is disrupted upon TCR activation. Interacts with
CC PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; mediates
CC the activation of SYK by SELPLG. Interacts with PDPN (via cytoplasmic
CC domain); activates RHOA and promotes epithelial-mesenchymal transition.
CC Interacts with SPN/CD43 cytoplasmic tail, CD44 and ICAM2 (By
CC similarity). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000250|UniProtKB:P26041}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26041};
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).
CC {ECO:0000250|UniProtKB:P26038, 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}.
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DR EMBL; M86450; AAB02864.1; -; mRNA.
DR PIR; S39804; S39804.
DR RefSeq; NP_001009578.1; NM_001009578.1.
DR AlphaFoldDB; P26042; -.
DR SMR; P26042; -.
DR STRING; 9823.ENSSSCP00000013160; -.
DR PaxDb; P26042; -.
DR PeptideAtlas; P26042; -.
DR PRIDE; P26042; -.
DR GeneID; 494458; -.
DR KEGG; ssc:494458; -.
DR CTD; 4478; -.
DR eggNOG; KOG3529; Eukaryota.
DR InParanoid; P26042; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0001771; P:immunological synapse formation; ISS:UniProtKB.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IBA:GO_Central.
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: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_0000219418"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 376..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..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 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; 67661 MW; 2C74AF0C81E73A9B CRC64;
MPKTINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
GMLREDAVLE YLKIAQDLEM YGVNYFSSKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQMER ALLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK
AQQELEEQTR RALALEQERK RAQSEAEKLA KERQEAEEAK EALLKASRDQ KKTQEQLALE
MAELTARISQ LEMARQKKES EAAEWQQKAQ MVQEDLEKTR AELKTAMSTP HGAEPAENDQ
DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
