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Database: UniProt
Entry: A0A1S3WIM4_ERIEU
LinkDB: A0A1S3WIM4_ERIEU
Original site: A0A1S3WIM4_ERIEU 
ID   A0A1S3WIM4_ERIEU        Unreviewed;       906 AA.
AC   A0A1S3WIM4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 isoform X2 {ECO:0000313|RefSeq:XP_016046132.1};
GN   Name=ASAP3 {ECO:0000313|RefSeq:XP_016046132.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046132.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046132.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_016046132.1; XM_016190646.1.
DR   AlphaFoldDB; A0A1S3WIM4; -.
DR   GeneID; 103118498; -.
DR   CTD; 55616; -.
DR   OrthoDB; 1449795at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IEA:InterPro.
DR   CDD; cd17900; ArfGap_ASAP3; 1.
DR   CDD; cd07640; BAR_ASAP3; 1.
DR   CDD; cd13251; PH_ASAP; 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   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; IPR047006; ASAP3_ArfGap.
DR   InterPro; IPR028775; BAR_ASAP3.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR037844; PH_ASAP.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR45854:SF1; ARF-GAP WITH SH3 DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 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   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 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   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          302..394
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          427..549
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          586..621
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          622..654
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          695..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  99951 MW;  ACAEB2E735DFE078 CRC64;
     MPKQFSVAEF LAVTVEDLSS PAGAAAFVAK MPRCRGAVLA REEILEGDQA ILQRIKKAVR
     MIHSSGLGHV ENEEQYQEAV ESLGNSHLSQ NSHELSTGFL NLSVFTREVA ALFKNLVQNL
     NNIVSFPLDS LLKGQLRDGR QDSKKQLEKA WKDYETKMTR LEKERDRARM SGGSPGELAH
     DTQRERRVFQ LHMCEYLLKA KESQMKQGPD FLQSLIKFFH AQHNFFQDGW KAAQSLSPFI
     EKLAVSVHAL RQAQEEELQN LTQLRDSLRG TLQLESREEN LNRKNSGGGY SIHQHQGNKQ
     FGTEKVGFLY KKSDGIRRVW QKRKCGIKYG CLTISHSTIN RPPVKLTLLT CQVRPNLEEK
     KCFDLVTHNR TYHFQAEDEH ECEAWVSVLQ NSKDEALSSA FLGEPSSSSL GPWGSAGLQG
     EPQDLTKLLI AEVKNRPGNN QCCDCGAADP TWLSTNLGVL TCIQCSGVHR ELGVRFSRMQ
     SLTLDLLGSS ELLLALNIGN TCFNEIMEAQ LPSHSGPKPS AESNMSARRD YIVAKYVEHR
     FARRSTLEPQ RLQMAICNQD LLSVLEAFAN GQDFRQPLLE PEGQAPGELA LHLAIRVANQ
     TSLPLVDFII QNGGHLDAKA ADGNSALHCA ALYNQPDCLK LLLKGRASVG SVNDSGETAL
     DIARKKQHKE CEELLEQAQA GTLAFPLHLD YSWEISTEPG SDSGEDEEEK QLCPLKPPTL
     AHWTNVRLDI SNKTYETITS LAPTAPQSQS EDFPPPLPVK NPSRSVVQER AGHGSRDWLE
     APSLSLEPFG VPENLSSPGS SSSSLMSPVE PGGPSKTLPG SEEGPRESPG PSKPSLISGT
     TLAETYHPVR FSSESTRSYR RGGRSLEDSS SSRQPLLKRN MPVGITEGDS SRAGGLPSSS
     MQPLQD
//
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