ID A0A2U3WLQ0_ODORO Unreviewed; 1128 AA.
AC A0A2U3WLQ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 isoform X1 {ECO:0000313|RefSeq:XP_004409890.1};
GN Name=ASAP1 {ECO:0000313|RefSeq:XP_004409890.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004409890.1};
RN [1] {ECO:0000313|RefSeq:XP_004409890.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_004409890.1; XM_004409833.1.
DR AlphaFoldDB; A0A2U3WLQ0; -.
DR STRING; 9708.A0A2U3WLQ0; -.
DR GeneID; 101369552; -.
DR KEGG; oro:101369552; -.
DR CTD; 50807; -.
DR InParanoid; A0A2U3WLQ0; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 320..412
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 435..558
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 596..631
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1066..1128
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 707..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..988
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 125245 MW; 8DBAF9625E9F9E83 CRC64;
MVSNLKRIMA HEPQKLMPDQ ISVSEFITET TEDYNSPTTS SFTTRLHNCR NTVTLLEEAL
DQDRTALQKV KKSVKAIYNS GQDHVQNEEN YAQVLDKFGS NFLSRDNPDL GTAFVKFSTL
TKELSTLLKN LLQGLSHNVI FTLDSLLKGD LKGVKGDLKK PFDKAWKDYE TKFTKIEKEK
REHAKQHGMI RTEITGAEIA EEMEKERRLF QLQMCEYLIK VNEIKTKKGV DLLQNLIKYY
HAQCNFFQDG LKTADKLKQY IEKLAADLYN IKQTQDEEKK QLTALRDLIK SSLQLDQKED
SQSRQGGYSM HQLQGNKEYG SEKKGYLLKK SDGLRKVWQR RKCAVKNGIL TISHATSNRQ
PAKLNLLTCQ VKPNAEDKKS FDLISHNRTY HFQAEDEQDY VAWISVLTNS KEEALTMAFR
GEQSTGENSL EDLTKAIIED VQRLPGNDVC CDCGSSEPTW LSTNLGILTC IECSGIHREM
GVHISRIQSL ELDKLGTSEL LLAKNVGNNS FNDIMEANLP SPSTKPTPSS DMTVRKEYIT
AKYVDHRFSR KACSSSSAKL NELLEAIKSR DLLALIQVYA EGVELMEPLL ESGQELGETA
LHLAVRTADQ TSLHLVDFLV QNCGNLDKQT ALGNTALHYC SMYSKPECLK LLLRSKPTVG
VVNQAGETAL DIAKRLKATQ CEDLLSQAKS GKFNPHVHVE YEWNLRQEEM DESDDDLDDK
PSPIKKERSP RPQSFCHSSS ISPQDKLSLP GFSTPRDKQR LSYGAFTNQI FVSTSTDSPT
SPTTEAPPLP PRNAGKGPTG PPSTLPLSTQ TSSGSSTLSK KRPPPPPPGH KRTLSDPPSP
LPHGPPNKGA VPWGNDVGPS SSSKTTNKFE GLSQQSSTGS AKTALGPRVL PKLPQKVALR
KTETSHHLSL DKASSPPEIF QKSSQLAELP QKPPPGDLPP KPSELAPKPQ IGDLPPKPGE
LPPKPQLGDL PPKPQLADLP PKPQMKDLPP KPQLGDLLAK SQTGEVSPKA QQPPDVTQKS
HPADLSPNVQ SRDAIQKQAS EDSNDLTPTL PETPVPLPRK INTGKNKVRR VKTIYDCQAD
NDDELTFMEG EVIVVTGEED QEWWIGHIEG QPERKGVFPV SFVHILSD
//
