ID A8WXS3_CAEBR Unreviewed; 659 AA.
AC A8WXS3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Protein CBR-GIT-1 {ECO:0000313|EMBL:CAP25197.2};
GN Name=git-1 {ECO:0000313|WormBase:CBG04486};
GN Synonyms=Cbr-git-1 {ECO:0000313|EMBL:CAP25197.2};
GN ORFNames=CBG04486 {ECO:0000313|WormBase:CBG04486}, CBG_04486
GN {ECO:0000313|EMBL:CAP25197.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP25197.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP25197.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP25197.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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DR EMBL; HE601277; CAP25197.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WXS3; -.
DR STRING; 6238.A8WXS3; -.
DR WormBase; CBG04486; CBP15074; WBGene00027149; Cbr-git-1.
DR eggNOG; KOG0818; Eukaryota.
DR HOGENOM; CLU_405575_0_0_1; -.
DR InParanoid; A8WXS3; -.
DR OMA; RENEVNW; -.
DR OrthoDB; 2877020at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0030056; C:hemidesmosome; IEA:EnsemblMetazoa.
DR GO; GO:0048786; C:presynaptic active zone; IEA:EnsemblMetazoa.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0035262; P:gonad morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0040039; P:inductive cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0036465; P:synaptic vesicle recycling; IBA:GO_Central.
DR CDD; cd08833; ArfGap_GIT; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR047161; GIT-like.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR PANTHER; PTHR46097:SF3; ARF GTPASE-ACTIVATING PROTEIN GIT; 1.
DR PANTHER; PTHR46097; G PROTEIN-COUPLED RECEPTOR KINASE INTERACTING ARFGAP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF08518; GIT_SHD; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 4..127
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 166..198
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 474..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 75463 MW; 3FBBEC72B3F11534 CRC64;
MYTAEALDLI TSLEQKECDD CGKREVEWAS VKKGTVICSE CFCFHSYLGP SVSYLRHLRK
SAWDEEHIRL VHALNSSNTN MIWESALYEG STKFQKPLAQ DPSHIKEQFV KEKYEKMTFQ
PKRGKDEDLE NSLNKQLIAC VRSDYAHVTL RLIALGADVN FLDPETGDTP LHVAARDGNC
NQVELLFLYG ADINAANKDG SLPYMVAKDY NHIQLSNRIY DFFFYTFDRF SFFMCNRKAD
HRNNQDFFIP EVTEKQFLIK TKDSRLAISV LPKGQFFDLC EDAFDETVRR ENEVNWNMTK
WAKTAKGPTN LFLPSTTHMS AARNQRRQKL AKFTPIQFTI LLIDLIKDQK RRINGDPLPI
QEAPRTQRKR NEYADYDEVA GISCSPTSGI LPNSQSNTVD ELNGRIWDEV LEMKERLLNA
ESMVLTVTKQ NEELTKLVHS LQAQNINLNS ELISFRDDLY NLKRTNMTRR MPSPLAIVET
PERILPPAGI QHSFSRRDSE DRVDGGGARW RSNSNDRRNS NDHKMEKKVE RRQDSMLESS
SSLSRSSQIP NSLNREDVKN RVIQQSEKIT RHIKALLQHG HNGNLDENAS HGAHEIACAI
NSLITVLLPY IRHEKIDSLT DAVVLLNAKC NSPILDSMDI IEAAQAVADK LRLIIMDFC
//
