ID Q6PBX2_DANRE Unreviewed; 198 AA.
AC Q6PBX2; A0A8M1N6M4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE SubName: Full=GTP-binding protein SAR1b {ECO:0000313|RefSeq:NP_001019548.1};
DE SubName: Full=SAR1a gene homolog 2 (S. cerevisiae) {ECO:0000313|EMBL:AAH59552.1};
DE SubName: Full=Secretion-associated, Ras-related GTPase 1B {ECO:0000313|Ensembl:ENSDARP00000136017};
GN Name=sar1b {ECO:0000313|Ensembl:ENSDARP00000136017,
GN ECO:0000313|RefSeq:NP_001019548.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-1958};
GN Synonyms=sara2 {ECO:0000313|EMBL:AAH59552.1,
GN ECO:0000313|RefSeq:NP_001019548.1}, zgc:73204
GN {ECO:0000313|RefSeq:NP_001019548.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH59552.1};
RN [1] {ECO:0000313|EMBL:AAH59552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Wild-type {ECO:0000313|EMBL:AAH59552.1};
RC TISSUE=Eye {ECO:0000313|EMBL:AAH59552.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001019548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001019548.1};
RX PubMed=17335798;
RA Davison J.M., Akitake C.M., Goll M.G., Rhee J.M., Gosse N., Baier H.,
RA Halpern M.E., Leach S.D., Parsons M.J.;
RT "Transactivation from Gal4-VP16 transgenic insertions for tissue-specific
RT cell labeling and ablation in zebrafish.";
RL Dev. Biol. 304:811-824(2007).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000136017, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000136017};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_001019548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001019548.1};
RX PubMed=25559265;
RA Levic D.S., Minkel J.R., Wang W.D., Rybski W.M., Melville D.B.,
RA Knapik E.W.;
RT "Animal model of Sar1b deficiency presents lipid absorption deficits
RT similar to Anderson disease.";
RL J. Mol. Med. 93:165-176(2015).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000136017}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000136017};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [6] {ECO:0000313|RefSeq:NP_001019548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001019548.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [7] {ECO:0000313|RefSeq:NP_001019548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001019548.1};
RX PubMed=29778665;
RA Saele O., Rod K.E.L., Quinlivan V.H., Li S., Farber S.A.;
RT "A novel system to quantify intestinal lipid digestion and transport.";
RL Biochim Biophys Acta Mol Cell Biol Lipids 1863:948-957(2018).
RN [8] {ECO:0000313|RefSeq:NP_001019548.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001019548.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000256|ARBA:ARBA00007507, ECO:0000256|RuleBase:RU003926}.
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DR EMBL; CU302316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059552; AAH59552.1; -; mRNA.
DR RefSeq; NP_001019548.1; NM_001024377.2.
DR STRING; 7955.ENSDARP00000136017; -.
DR PaxDb; 7955-ENSDARP00000124511; -.
DR Ensembl; ENSDART00000162422.2; ENSDARP00000136017.1; ENSDARG00000103403.2.
DR GeneID; 554177; -.
DR KEGG; dre:554177; -.
DR AGR; ZFIN:ZDB-GENE-040426-1958; -.
DR CTD; 51128; -.
DR ZFIN; ZDB-GENE-040426-1958; sar1b.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR OMA; GLWNKHG; -.
DR OrthoDB; 5349301at2759; -.
DR TreeFam; TF312890; -.
DR Reactome; R-DRE-204005; COPII-mediated vesicle transport.
DR Reactome; R-DRE-2132295; MHC class II antigen presentation.
DR Reactome; R-DRE-5694530; Cargo concentration in the ER.
DR Reactome; R-DRE-8963888; Chylomicron assembly.
DR Reactome; R-DRE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR Proteomes; UP000000437; Chromosome 21.
DR Bgee; ENSDARG00000103403; Expressed in zone of skin and 35 other cell types or tissues.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:ZFIN.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0035265; P:organ growth; IMP:ZFIN.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
DR CDD; cd00879; Sar1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR006687; Small_GTPase_SAR1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR45684:SF40; GTP-BINDING PROTEIN SAR1B; 1.
DR PANTHER; PTHR45684; RE74312P; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51422; SAR1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU003926};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU003926};
KW Golgi apparatus {ECO:0000256|RuleBase:RU003926};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|RuleBase:RU003926};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q6PBX2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transport {ECO:0000256|RuleBase:RU003926}.
SQ SEQUENCE 198 AA; 22229 MW; 72D15A5CCF4C2967 CRC64;
MSFIFDWIYS GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHA QARRVWKNYL PAINGIVFLV DCIDHGRLAE SKTELDALMT
DETIGNVPIL ILGNKIDKPE AISEEKLREI FGLYGQTTGK GNIPLKELNT RPLEVFMCSV
LKRQGYGEGF RWLSQYID
//
