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Database: UniProt
Entry: C0H9V0_SALSA
LinkDB: C0H9V0_SALSA
Original site: C0H9V0_SALSA 
ID   C0H9V0_SALSA            Unreviewed;       545 AA.
AC   C0H9V0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 3 {ECO:0000256|ARBA:ARBA00039243};
GN   Name=ARFG3 {ECO:0000313|EMBL:ACN10819.1};
GN   Synonyms=LOC106576371 {ECO:0000313|RefSeq:XP_014008977.1};
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|EMBL:ACN10819.1};
RN   [1] {ECO:0000313|EMBL:ACN10819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10819.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACN10819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10819.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACN10819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACN10819.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:XP_014008977.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014008977.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane
CC       protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}.
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DR   EMBL; BT059106; ACN10819.1; -; mRNA.
DR   RefSeq; XP_014008977.1; XM_014153502.1.
DR   STRING; 8030.ENSSSAP00000022553; -.
DR   PaxDb; 8030-ENSSSAP00000022553; -.
DR   GeneID; 106576371; -.
DR   KEGG; sasa:106576371; -.
DR   OMA; ENGPSKV; -.
DR   OrthoDB; 389572at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa17.
DR   Bgee; ENSSSAG00000014750; Expressed in ovary and 15 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR   PANTHER; PTHR45686:SF1; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN 3; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          10..126
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          163..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  59957 MW;  0F5A16B44E960400 CRC64;
     MSEPSKQDIA AIFKRLRSLS TNKVCFDCSA KNPSWASITY GVFLCIDCSG THRSLGVHLS
     FIRSTELDSN WSWYQLRCMQ VGGNASANAF FAQQGCTSNA ANTKYNSRAA VLYREKIKTS
     ATQATRRFGT ELWLDSQAPL SPTSPVNKEE DFFSMHVQAF PDDRSSAQPN ITSSAQMNLS
     PTPVEEPSTK ETEREKNGNT EGPSVDVLSM SPKEALESSL LKKKPAGAKK TLGAKKGGLG
     GKKVSKQSFC DLEKKAQAVD KLNERDTAPT TTKNSPQPAE ESIGASMRLA YKDLEAQQRS
     NTEKMKGMGE KKKEQAERLG MGFGSRSGVS HSVLSDMHTI QQESPVGSKQ PTKSRRYTEK
     EEEETDEGSF TSRMSMTSSM TKFDEPTESS DKFFSNWSET GESGWRKESR KPEPDFYLST
     KSSSQDDRTA ARRKADPVPV SDSGDARKKF GDVKAISSDM YFGKQDDSEY EAKTRLERFS
     GSNSISSADL FDDPKKQMAS SYRLTNMLPS APDMSQLKLG VRSAAGRLSV MASGVVTSLQ
     DHYSA
//
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