GenomeNet

Database: UniProt
Entry: A0A3Q3LJK3_9LABR
LinkDB: A0A3Q3LJK3_9LABR
Original site: A0A3Q3LJK3_9LABR 
ID   A0A3Q3LJK3_9LABR        Unreviewed;       760 AA.
AC   A0A3Q3LJK3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=GIT ArfGAP 2 {ECO:0000313|Ensembl:ENSLBEP00000008985.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000008985.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000008985.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3Q3LJK3; -.
DR   STRING; 56723.ENSLBEP00000008985; -.
DR   Ensembl; ENSLBET00000009472.1; ENSLBEP00000008985.1; ENSLBEG00000006895.1.
DR   GeneTree; ENSGT00940000156383; -.
DR   InParanoid; A0A3Q3LJK3; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IEA:InterPro.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR   Gene3D; 1.20.5.170; -; 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; IPR032352; GIT1/2_CC.
DR   InterPro; IPR022018; GIT1_C.
DR   InterPro; IPR013724; GIT_SHD.
DR   PANTHER; PTHR46097:SF4; ARF GTPASE-ACTIVATING PROTEIN GIT2; 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; PF16559; GIT_CC; 1.
DR   Pfam; PF08518; GIT_SHD; 2.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          1..124
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          380..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        402..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  84960 MW;  D4F328C6D8FD74C2 CRC64;
     MSKRLRNTEL CADCSVPEPR WASVNRGVLI CDECCSVHRS LGRHSSQVRH LTHTPWPTTQ
     LQMVQTLYSN GANSIWEHSL LDPASVMSGK RKANPQDKLH PNKSEFIRAK YQMLAFVHRM
     PCREDDSSTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGNTP LHVAAKAGQV
     SQAELLTVYG ADPGAPDSNG KTPIDYAREA GHHDLADRLV EVQYELTDRL AFYLCGRKPD
     HKSGQHFIVP QMADSSLDLS ELAKAAKKKL QALSNHLFEE LAMDVYDEVD RRETDAVWLA
     TQNHSTLVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL SDAKRRQQGN
     MISSPKDNVE FILKSMAVRR CSDSQDNDQP DYDSVASDED TDQELPSSKG DRTKSLDSDL
     SDSPITMQEY LEVKNALSAS EAKIQHLMKA NNNLSDELRL MQKKLQSLKS ENTSLRRQVT
     TNIYQVPSGS DYPDPSSPSA LKRRQSARAS RPMSMYETGS GLKPFHPKGE NPYPEEALPN
     LQPFPPHKER GAFVTTSSSL PSFPSTLSWP RDESVQKAPK LEKQSSMPES DYDNTFNDSE
     MEDSSLCRRA RLRSSGWMGE GSSIPELADV EMEPDPTLPS TEDVIRKTEQ ITKNIQELLR
     AAQENKHDSF IPCSERIHVA VTEMAALFPK KPRSETVRGS LRLLTSSAYR LQSECRKALP
     SEGCPGPDMQ LVTQQVIQCA YDIAKAAKQL VTITTKENTH
//
DBGET integrated database retrieval system