ID A0A0D9RGB1_CHLSB Unreviewed; 895 AA.
AC A0A0D9RGB1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ras and Rab interactor 2 {ECO:0000313|Ensembl:ENSCSAP00000007650.1};
GN Name=RIN2 {ECO:0000313|Ensembl:ENSCSAP00000007650.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000007650.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000007650.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000007650.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AQIB01145293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007959485.1; XM_007961294.1.
DR RefSeq; XP_007959494.1; XM_007961303.1.
DR RefSeq; XP_007959498.1; XM_007961307.1.
DR RefSeq; XP_007959503.1; XM_007961312.1.
DR RefSeq; XP_007959513.1; XM_007961322.1.
DR RefSeq; XP_007959520.1; XM_007961329.1.
DR AlphaFoldDB; A0A0D9RGB1; -.
DR STRING; 60711.ENSCSAP00000007650; -.
DR Ensembl; ENSCSAT00000009537.1; ENSCSAP00000007650.1; ENSCSAG00000011446.1.
DR GeneID; 103215085; -.
DR CTD; 54453; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000154866; -.
DR OMA; CISRKIR; -.
DR OrthoDB; 5483004at2759; -.
DR BioGRID-ORCS; 103215085; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 2.
DR Bgee; ENSCSAG00000011446; Expressed in fibroblast and 7 other cell types or tissues.
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:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; IEA:Ensembl.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16131; RA_Rin2; 1.
DR CDD; cd10394; SH2_RIN2; 1.
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; IPR035868; RIN2_SH2.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 97..190
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 618..757
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT DOMAIN 787..878
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 212..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 100076 MW; 983A405BA4B3D608 CRC64;
MSAWTMGARG LDKRGSFFKL IDTIASEIGE LKQEMVRTDV SLENGLEPAE THSMVRHKDG
GYSEEEDVKT CARDSGYDSL SNRLSILDRL LHTHPIWLQL GLSEEEAAEV LQAQPPGIFL
VHKSTKMQKK VLSLRLPCEF GAPLKEFAIK ESTYTFSLEG SGISFADLFR LIAFYCISRD
VLPFTLKLPY AISTAKSEAQ LEELAQMGLN FWSSPADSKP PNPPPPHRPL SSDGICPASL
RQLCLINGVH SIKTRTPSEL ECSQTNGALC FINPLFLKVH SQDLSGGLKR PSTRTPNANG
TERTRSPPPR PPPPAINSLH TSPRLARTET QTSMPETVNH NKHGNVALPG TKPTPIPPPR
LKKQASFLEA EGGAKTLSGG RPGAGPELEL GTAGSPGGAP PEAAPGDCTR APPPSSESRP
PCHGGRQRLS DMSISTSSSD SLEFDRSMPL FGYEADTNSS LEDYEGESDQ ETMAPPIKSK
KKRSSSFVLP KLVKSQLQKV SGVFSSFMTP EKRMVRRIAE LSRDKCTYFG CLVQDYVSFL
QENKECHVSS TDMLQTIRQF MTQVKNYLSQ SSELDPPIES LIPEDQIDVV LEKAMHKCIL
KPLKGHVEAM LKDFHMADGS WKQLKENLQL VRQRNPQELG VFAPTPDFVD VEKIKVKFMT
MQKMYSPEKK VMLLLRVCKL IYTVMENNSG RMYGADDFLP VLTYVIAQCD MLELDTEIEY
MMELLDPSLL HGEGGYYLTS AYGALSLIKN FQEEQAARLL SSETRDTLRQ WHKRRTTNRT
IPSVDDFQNY LRVAFQEVNS GCTGKTLLVR PYITTEDVCQ ICAEKFKVGD PEEYSLFLFV
DETWQQLAED TYPQKIKAEL HSRPQPHIFH FVYKRIKNDP YGVIFQNGEE DLTTS
//
