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Database: UniProt
Entry: H0VR71_CAVPO
LinkDB: H0VR71_CAVPO
Original site: H0VR71_CAVPO 
ID   H0VR71_CAVPO            Unreviewed;       563 AA.
AC   H0VR71;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Neurofibromin 2 {ECO:0000313|Ensembl:ENSCPOP00000013070.3};
GN   Name=NF2 {ECO:0000313|Ensembl:ENSCPOP00000013070.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013070.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000013070.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013070.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC       cytoskeleton {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   EMBL; AAKN02007267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02007268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02007269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0VR71; -.
DR   Ensembl; ENSCPOT00000014649.3; ENSCPOP00000013070.3; ENSCPOG00000014504.4.
DR   VEuPathDB; HostDB:ENSCPOG00000014504; -.
DR   eggNOG; KOG3529; Eukaryota.
DR   GeneTree; ENSGT01020000230354; -.
DR   HOGENOM; CLU_003623_6_1_1; -.
DR   TreeFam; TF313935; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000014504; Expressed in heart left ventricle and 12 other cell types or tissues.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   CDD; cd17186; FERM_F1_Merlin; 1.
DR   Gene3D; 1.20.5.450; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.20.80.60; -; 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:SF23; MERLIN; 1.
DR   PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 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; 2.
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   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   DOMAIN          1..283
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          303..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          490..531
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        537..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76..79
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         266
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   563 AA;  65964 MW;  6877D3ECA12CD844 CRC64;
     MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV CRTLGLRETW
     FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF YPENAEEELV QESTQHLFFL
     QYGDYDPSLH KLGFLAQEEL LPKRVINLYQ MTPEMWEERI TAWYAGHRGR ARDEAEMEYL
     KIAQDLEMYG VNYFAIRNKK GTELLLGVDA LGLHIYDPEN RLTPKISFPW NEIRNISYSD
     KEFTIKPLDK KIDVFKFNSS KLRVNKLILQ LCIGNHDLFM RRRKADSLEV QQMKAQAREE
     KARKQMERQR LAREKQMREE AERSRDELER RLLQMKEEAT MANEALMRSE ETADLLAEKA
     QITEEEAKLL AQKAAEAEQE MQRIKATAIR TEEEKRLMEQ KVLEAEVLAL KMAEESERRA
     KEADQLKQDL QEAREAERRA KQKLLEIATK PTYLPVNPIP APMPPDIPSF NLIGDSLSFD
     FKDTDMKRLS MEIEKEKVEY MEKSKHLQEQ LNELKTEIEA LKLKERETAL DILHNENSDR
     GGTSSKHNTI KKPQAQGRRP ICI
//
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