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Database: UniProt
Entry: A0A3B1JHV2_ASTMX
LinkDB: A0A3B1JHV2_ASTMX
Original site: A0A3B1JHV2_ASTMX 
ID   A0A3B1JHV2_ASTMX        Unreviewed;      1167 AA.
AC   A0A3B1JHV2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ArfGAP with SH3 domain, ankyrin repeat and PH domain 1b {ECO:0000313|Ensembl:ENSAMXP00000041997.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000041997.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000041997.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B1JHV2; -.
DR   Ensembl; ENSAMXT00000030326.1; ENSAMXP00000041997.1; ENSAMXG00000002685.2.
DR   GeneTree; ENSGT00940000158547; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000002685; Expressed in camera-type eye and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08848; ArfGap_ASAP1; 1.
DR   CDD; cd07641; BAR_ASAP1; 1.
DR   CDD; cd13251; PH_ASAP; 1.
DR   CDD; cd11965; SH3_ASAP1; 1.
DR   Gene3D; 1.25.40.950; -; 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; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
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; IPR043593; ASAP.
DR   InterPro; IPR037928; ASAP1_BAR.
DR   InterPro; IPR038016; ASAP1_SH3.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR037844; PH_ASAP.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR45854:SF2; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45854; ASAP FAMILY MEMBER; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          334..426
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          449..562
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          610..645
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1105..1167
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          721..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..869
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..894
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..948
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..1025
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1056
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1080
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1167 AA;  130148 MW;  93BDBB82C019C018 CRC64;
     MSQVLQVGRE VMRSSSSRLS SFSSKDCLWN RMPDQISVSE FLSETTEDYN SPTTSSFTTR
     LQSCRNTVSV LEEALDQDRT SLQKVKKSVK AIYNSGQDHV QNEETYALAL DKFGSNFISR
     DNPDLGTAFV KFSTLTKELS ALLKNLLQSL SHNVIFTLDS LLKGDLKGVK GDLKKPFDKA
     WKDYETKFTK IEKEKREHAK QHGMIRTEIT GAEIAEEMEK ERRLFQLQMC EYLIKVNEIK
     TKKGVDLLQN LIKYYHAQCN FFQDGLKTAD KLKQYIEKLA ADLYNIKQTQ DEEKKQLTAL
     RDLIKSSLQL EKEDSQSKQG GYSMHQLQGN KEFGSEKKGY LMKKSDGLRK VWQRRKCSVK
     GGILTISHAT SNRQPVKLNL LTCQVKPSAE DRKCFDLISH NRTYHFQAED EQEFVIWISV
     LTNSKEEALN MAFRGEQTAG EDGLEDLTKA IIDDVLRIPG NEVCCDCGAA DPKWLSTNLG
     ILTCIECSGI HREMGVHISR IQSMELDKLG TSELLLAKNV GNSNFNEIME GNLPCPSPKP
     TPSSDMTVRK EFIHAKYVDH KFARKMCMSA AVKMSELYEA VRSRDLLALI QVYAEGVELM
     EPLPDAGQEA GETALHFAVR TADHTSLHQV DFLVQNSGNL DKQTERGNTA LHYCCIYEKH
     ECLKLLLRGK PATDITNHNG ETALDVARRM RIDQCAEALM QATEGKFNPK VHVEYEWNLR
     QEEMDESDDD LDDKPSPIKK DRRPQSFCHS SSLSPHDKLS LPIFSGPRDK QRLSYSSFTT
     QMYSVSTDCP SSPVSDAPPL PPRNAGKAPP LAFLGSHSHY ATLASTRLYI TPPSSSSPLS
     PGSQIPSNSN STLSKKRPPP PPPGHKRTLS DPPTPLSYTP HCKGSDSTPP PINKMSPVAN
     RFEGILQQQS TTSSTTKSTL GPRVLPKLPQ KVALRKIETI HHPSVDRPSQ PHEPVLLFQK
     SLQCSDTPQK VPVPDKPHSG DLPPKPQPSE LPPKPGELPP KPHLSDLPPK PQLGDLPPKP
     QLKDLPPKPQ LADLPILKPV APEPVHKPPP GEVTPKSESP ETPTSIQPAE PSPQPTPPSE
     DTNGSPACAP DTPVPLPRKI NTGKSKTRRV KTIYDCQADN DDELTFVEGE VIVVTGEEDQ
     EWWIGHIEGQ PERKGAFPMS FVHILSD
//
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