(data stored in ACNUC9306 zone)

HOGENOM: PIGX_53_PE1

ID   PIGX_53_PE1                          STANDARD;      PRT;   577 AA.
AC   PIGX_53_PE1; P26042;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Moesin;AltName: Full=Membrane-organizing extension spike
DE   protein; (PIGX_53.PE1).
GN   Name=MSN;
OS   SUS SCROFA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PIGX_53.PE1.
CC       Sus scrofa chromosome X Sscrofa9 partial sequence 51245310..52245309
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:MOES_PIG
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane.
CC   -!- ENZYME REGULATION: A head-to-tail association, of the N-terminal
CC       and C-terminal halves results in a closed conformation (inactive
CC       form) which is incapable of actin or membrane-binding (By
CC       similarity).
CC   -!- SUBUNIT: Binds SLC9A3R1. In resting T-cells, part of a PAG1-
CC       SLC9A3R1-MSN complex which is disrupted upon TCR activation.
CC       Interacts with PPP1R16B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Apical cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cell projection, microvillus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Phosphorylated form is enriched in microvilli-
CC       like structures at apical membrane. Increased cell membrane
CC       localization of both phosphorylated and non-phosphorylated forms
CC       seen after thrombin treatment (By similarity).
CC   -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC       microvilli-like structures. Phosphorylation by ROCK2 suppresses
CC       the head-to-tail association of the N-terminal and C-terminal
CC       halves resulting in an opened conformation which is capable of
CC       actin and membrane-binding (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Sus_scrofa;ENSSSCG00000012365;ENSSSCT00000013522;ENSSSCP00000013160.
DR   EMBL; M86450; - ;
DR   UniProtKB/Swiss-Prot; P26042; -.
DR   EMBL; M86450; AAB02864.1; -; mRNA.
DR   PIR; S39804; S39804.
DR   RefSeq; NP_001009578.1; NM_001009578.1.
DR   UniGene; Ssc.14470; -.
DR   ProteinModelPortal; P26042; -.
DR   SMR; P26042; 1-385, 488-577.
DR   STRING; P26042; -.
DR   GeneID; 494458; -.
DR   KEGG; ssc:494458; -.
DR   CTD; 4478; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   OrthoDB; EOG4C5CJJ; -.
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:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00769; ERM; 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   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF48678; Moesin; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   HOGENOMDNA; PIGX_53.PE1; -.
KW   ENSSSCG00000012365820036002503210000011;
KW   MOES_PIG; M86450;
KW   Acetylation; Cell membrane; Cell projection; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
SQ   SEQUENCE   577 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKTINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKGFSTWLK
     LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE
     TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
     GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQMER ALLENEKKKR EMAEKEKEKI EREKEELMER LKQIEEQTKK
     AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLKASRDQ KKTQEQLALE
     MAELTARISQ LEMARQKKES EAAEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENDQ
     DEQDENGAEA SADLRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA
     NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
//

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