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Database: UniProt
Entry: A0A1S3PQ23_SALSA
LinkDB: A0A1S3PQ23_SALSA
Original site: A0A1S3PQ23_SALSA 
ID   A0A1S3PQ23_SALSA        Unreviewed;      1039 AA.
AC   A0A1S3PQ23;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Ras and Rab interactor 2-like isoform X1 {ECO:0000313|RefSeq:XP_014029768.1};
GN   Name=LOC106586723 {ECO:0000313|RefSeq:XP_014029768.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014029768.1};
RN   [1] {ECO:0000313|RefSeq:XP_014029768.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014029768.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC       {ECO:0000256|ARBA:ARBA00006919}.
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DR   RefSeq; XP_014029768.1; XM_014174293.1.
DR   AlphaFoldDB; A0A1S3PQ23; -.
DR   GeneID; 106586723; -.
DR   KEGG; sasa:106586723; -.
DR   OrthoDB; 5483004at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR045046; Vps9-like.
DR   InterPro; IPR037191; VPS9_dom_sf.
DR   PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR23101:SF51; RAS AND RAB INTERACTOR 2; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF109993; VPS9 domain; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   3: Inferred from homology;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT   DOMAIN          139..235
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          751..891
FT                   /note="VPS9"
FT                   /evidence="ECO:0000259|PROSITE:PS51205"
FT   DOMAIN          921..1012
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..418
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  115106 MW;  9C06C1B61079A113 CRC64;
     MAATLPSTLH STLPRPDCHM DRSGSFFKDS DGLTDSDLSM SATLPRPDCH MDRRGSFFKL
     IDTFALEIGE LKQEMVQTSP TEDRDPYPMV LQGLEGEVSG VYLQSSPCAG ASGERDSGYD
     SLRRRMSVLD RLRHTHPVWL LLTLSDTEAT RILLQQPPGV FLVRKSSTLQ RKVLSLRVSE
     DDASGGASVC DFPVRESQYT FSLEGSGISF ADLFRLVAFY CISRDILPFT LNLPEAIAAS
     KTQKDLEEVA QLGAGFWHSA LGSLRRTTSP SRPPPQRPDR DGDNQGAERT QEKQSVTRHS
     SVPPAFPPSS SSSRLERSQS NGALCFVNPL FLQTHRRLEE DPQSSSTSPS PYVTHSTPSP
     GTTGGTSSAP VTDPNVKRKS RPPRPPPPRS LLVPPPRSLS QRRQAPPPPT PLPQKPKSSM
     PETPAAIVVT RQPLQPSSNQ NLRPTPRPPM GARHSSHSKK TTSSAAMPVP HHHPQHPPPP
     RPKKPDIDAH RCHIALDDET IAKALSRAKL PPCQAPAIVG NGAGSPPSPP GKTPRREGQE
     GRLSDMSIST SSSDSLDYSH PPLSLPASPP LRLRHHLGNN EDSSDDEDLC DEEEEDYGVS
     LENDLDQGLR PPFKARRRGV GVGVKVALSF RKVSGVFSTF MTPERRAVRR IAALSRDKSS
     YFGCLVQDYI SFVQENKGCH TSGLDLLQTL RQFMTQMKAY LTQSSELDPP IESLIPEDQI
     DTVLEKAMHK CVLKPLKGVV EVALHDFQVS SGGWQQLREN LALAKTRRPQ DLGVDGAVPP
     DPMAIEKIRH KFHNMRKMYS PDKKVSLLLR VCKLIYTIMQ DNSGRMYGAD DFLPMLTYVL
     AQCDMPQLDT EILYMMELLD PSLLHGEGGY YLTSAYGAMA LIKNFQEEQA ARVLSSEARD
     TLHQWHRRRT AQRTAPSVDD FQNYLRVALQ EVNSGCTAKT LLVHPYSTTE EVCSLCTYKF
     KVHDPENHAL FLITEATSQQ LAPDTHPQRI KAEIHSHPNS QPFHFVYRRV PNLNLCIPAI
     PANQHNGNCL LPSQLDELN
//
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