ID A0A3B4UVQ6_SERDU Unreviewed; 1090 AA.
AC A0A3B4UVQ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Ras and Rab interactor 2-like {ECO:0000313|Ensembl:ENSSDUP00000022558.1};
GN Name=RIN2 {ECO:0000313|Ensembl:ENSSDUP00000022558.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000022558.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000022558.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000256|ARBA:ARBA00006919}.
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DR AlphaFoldDB; A0A3B4UVQ6; -.
DR STRING; 41447.ENSSDUP00000022558; -.
DR Ensembl; ENSSDUT00000022973.1; ENSSDUP00000022558.1; ENSSDUG00000016426.1.
DR GeneTree; ENSGT00940000154866; -.
DR OMA; MAFCCIS; -.
DR Proteomes; UP000261420; Unplaced.
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:1903670; P:regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
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; IPR029071; Ubiquitin-like_domsf.
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; SSF54236; Ubiquitin-like; 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 SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 102..195
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 770..910
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT DOMAIN 940..1031
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..608
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 120499 MW; CD9A65EB0BD94206 CRC64;
MSSVSPPCRQ ERKGSFFKLI DSFAWELGTL KKELGKQPKP AEEDHSTDPV FRLSEEVRGL
FLQPSPCAGI RAGPAGARDS GYDSLHRRLS VLDRLVHTHA VWLQLSLSHQ DAMLLLQNQE
AGMFVVRRSA SLQRKVISLR MDQDSEEPVR DFPVRESQYT FSLEGSGLSF ADLFRLVAFC
CISRDVLPFT LKLPDVIASA TTSADLEEVA KLGPGFWDTQ LCRRRKDSVP VSVTSAPDRL
PSPAQTSVSL ATGHSRLQTR TPTELECCQS NGALCFINPL FIKVHQPQSD QSTTPDPSDT
TQQGLREYPV INNRDGPQVW SSGLRDLQSL SKTTDLQDDT SHTSSSQKQS AAEAVSRSPP
PRPPPPRFVS RCSAPPVRQR SMPEKISWIN IPKEKVEERE RGSSLLSRLG SSLSISPSSS
PPKRLSISSP ISISRPSLPL SLSSLSSSPR RAKASPSSSQ EDAQCHLALE EQTIEKALIK
ARLSQSSGTR SSTQDSSSPP QQSLMTAMKQ SEIPGGEEEA SEDCSGGGQR LSDMSLSTDS
SDSLDFSQSS AFFLPPLHDP SPPTTADLNT HLPLSIPPSH LPYCSIEDDD DDDEEDEDEA
DYGVSLESDQ DQDQDLTMVP PGHRTNRRPS AGALVLQKAL RGHLRKMSGV FNSLLTPEKR
AVRRVLELSR DKGSYFGSLV QDYLSYMGEG AGTQAWQGYA SGLELLQTLR QFITQMKSYL
RQSSEMEPPI ESLIPEDQID QVLEKAMHKC VLKPLKPVVS AALQEFQVRS GEWQELKENL
SLAKARQPQD MGVADTLPPD QVAIEKIRHK FHTMCKLYSP EKKVSTLLRV CKLIYTIMED
NSGRLYGADD FLPMLTYVLA QCDMPQLDNE ILYMMELLDP SQLHGEGGYY LTSAYGAMSL
IRNFQEEQAA RVLSSETRDT LHQWHRRRTT QRSAPSIDDF QNYLRVALQE LDSGCTAKTL
QVRPYATVDE VCQLCAQKFK VSDPQDYGLF LLMEGSSQQL APDTHPQKIK AELHSRPQPP
PFHFVFRRVA NSSTLTSATP NLNNLTVTSD PQDNLNDLSR DLTGSSPQST LSLGLCPALS
LSLAGGGLEV
//
