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Database: UniProt
Entry: F6PUX2_HORSE
LinkDB: F6PUX2_HORSE
Original site: F6PUX2_HORSE 
ID   F6PUX2_HORSE            Unreviewed;       549 AA.
AC   F6PUX2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Moesin {ECO:0000256|ARBA:ARBA00041051};
DE   AltName: Full=Membrane-organizing extension spike protein {ECO:0000256|ARBA:ARBA00043042};
GN   Name=MSN {ECO:0000313|VGNC:VGNC:20392};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000010937.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000010937.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010937.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000010937.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010937.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, microvillus
CC       {ECO:0000256|ARBA:ARBA00004105}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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DR   AlphaFoldDB; F6PUX2; -.
DR   Ensembl; ENSECAT00000013753.3; ENSECAP00000010937.2; ENSECAG00000012900.4.
DR   CTD; 4478; -.
DR   VGNC; VGNC:20392; MSN.
DR   GeneTree; ENSGT01090000260082; -.
DR   HOGENOM; CLU_003623_6_2_1; -.
DR   OrthoDB; 5476297at2759; -.
DR   TreeFam; TF313935; -.
DR   Proteomes; UP000002281; Chromosome X.
DR   Bgee; ENSECAG00000012900; Expressed in synovial membrane of synovial joint and 23 other cell types or tissues.
DR   ExpressionAtlas; F6PUX2; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.5.450; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 6.10.360.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C_dom.
DR   InterPro; IPR041789; ERM_FERM_C.
DR   InterPro; IPR046810; ERM_helical.
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; MERLIN/MOESIN/EZRIN/RADIXIN; 1.
DR   PANTHER; PTHR23281:SF26; MOESIN; 1.
DR   Pfam; PF00769; ERM_C; 1.
DR   Pfam; PF20492; ERM_helical; 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; SSF48678; Moesin tail domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F6PUX2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT   DOMAIN          1..267
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          347..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..35
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
FT   BINDING         250
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol)"
FT                   /ligand_id="ChEBI:CHEBI:57880"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
SQ   SEQUENCE   549 AA;  64592 MW;  2E3D6C625976A828 CRC64;
     MPKTVVKTIG LREVWFFGLQ YQDTKGFSTW LKLNKKVTAQ DVRKESPLLF KFRAKFYPED
     VSEELIQDIT QRLFFLQVKE GILNDDIYCP PETAVLLASY AVQSKYGDFN KEVHKSGYLA
     GDKLLPQRVL EQHKLNKDQW EERIQVWHEE HRGMLREDAV LEYLKIAQDL EMYGVNYFSI
     KNKKGSELWL GVDALGLNIY EQNDRLTPKI GFPWSEIRNI SFNDKKFVIK PIDKKAPDFV
     FYAPRLRINK RILALCMGNH ELYMRRRKPD TIEVQQMKAQ AREEKHQKQM ERALLENEKK
     KREMAEKEKE KIEREKEELM ERLKQIEEQT KKAQQELEEQ TRRALELEQE RKRAQSEAEK
     LAKERQEAEE AKEALLQASQ DQKKTQEQLA LEMAELTARI SQLEVARQKK ESEAVEWQQK
     AQMVQEDLEK TRAELKTAMS TPHVAEPAEN DQDEQDENGA EASADLRADA MAKDRSEEER
     TTEAEKNERV QKHLKALTSE LANARDESKK TANDMIHAEN MRLGRDKYKT LRQIRQGNTK
     QRIDEFESM
//
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