ASAP1_MOUSE
ID ASAP1_MOUSE Reviewed; 1147 AA.
AC Q9QWY8; O08612; Q505F0; Q80TG8; Q80UV6; Q99LV8; Q9Z2B6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein;
DE AltName: Full=ADP-ribosylation factor-directed GTPase-activating protein 1;
DE Short=ARF GTPase-activating protein 1;
DE AltName: Full=Development and differentiation-enhancing factor 1;
DE Short=DEF-1;
DE Short=Differentiation-enhancing factor 1;
DE AltName: Full=PIP2-dependent ARF1 GAP;
GN Name=Asap1; Synonyms=Ddef1, Kiaa1249, Shag1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, AND
RP MUTAGENESIS OF ARG-811; PRO-910 AND PRO-913.
RC TISSUE=Brain, and Embryo;
RX PubMed=9819391; DOI=10.1128/mcb.18.12.7038;
RA Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA Randazzo P.A.;
RT "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT associates with and is phosphorylated by Src.";
RL Mol. Cell. Biol. 18:7038-7051(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 20-1147 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1147 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 654-1147 (ISOFORM 1).
RX PubMed=9126384; DOI=10.1006/abio.1997.2040;
RA Yamabhai M., Kay B.K.;
RT "Examining the specificity of Src homology 3 domain -- ligand interactions
RT with alkaline phosphatase fusion proteins.";
RL Anal. Biochem. 247:143-151(1997).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10022919; DOI=10.1128/mcb.19.3.2330;
RA King F.J., Hu E., Harris D.F., Sarraf P., Spiegelman B.M., Roberts T.M.;
RT "DEF-1, a novel src SH3 binding protein that promotes adipogenesis in
RT fibroblastic cell lines.";
RL Mol. Cell. Biol. 19:2330-2337(1999).
RN [7]
RP INTERACTION WITH REPS2.
RX PubMed=12149250; DOI=10.1074/jbc.m203453200;
RA Oshiro T., Koyama S., Sugiyama S., Kondo A., Onodera Y., Asahara T.,
RA Sabe H., Kikuchi A.;
RT "Interaction of POB1, a downstream molecule of small G protein Ral, with
RT PAG2, a paxillin-binding protein, is involved in cell migration.";
RL J. Biol. Chem. 277:38618-38626(2002).
RN [8]
RP PHOSPHORYLATION AT TYR-308, AND INTERACTION WITH PTK2B/PYK2.
RX PubMed=12771146; DOI=10.1074/jbc.m302278200;
RA Kruljac-Letunic A., Moelleken J., Kallin A., Wieland F., Blaukat A.;
RT "The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and
RT inhibition of the Arf-GTPase-activating protein ASAP1.";
RL J. Biol. Chem. 278:29560-29570(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732 AND SER-858, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP INTERACTION WITH RAB11FIP3.
RX PubMed=18685082; DOI=10.1091/mbc.e08-03-0290;
RA Inoue H., Ha V.L., Prekeris R., Randazzo P.A.;
RT "Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and
RT regulates pericentrosomal localization of transferrin receptor-positive
RT recycling endosome.";
RL Mol. Biol. Cell 19:4224-4237(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732; SER-858; SER-1045;
RP SER-1059; THR-1066 AND SER-1146, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a signal transduction protein involved in the
CC differentiation of fibroblasts into adipocytes and possibly other cell
CC types. Plays a role in ciliogenesis (By similarity). Posseses
CC phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating
CC protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a
CC lesser activity towards ARF6. May coordinate membrane trafficking with
CC cell growth or actin cytoskeleton remodeling by binding to both SRC and
CC PIP2. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Activity stimulated by phosphatidylinositol 4,5-
CC bisphosphate (PIP2).
CC -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC RAB11FIP3. Interacts with PTK2B/PYK2. Interacts with REPS2; the
CC interaction is direct (PubMed:12149250). {ECO:0000269|PubMed:12149250,
CC ECO:0000269|PubMed:12771146, ECO:0000269|PubMed:18685082}.
CC -!- INTERACTION:
CC Q9QWY8-1; P00523: SRC; Xeno; NbExp=3; IntAct=EBI-698517, EBI-848039;
CC Q9QWY8-2; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-698524, EBI-848039;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Predominantly
CC cytoplasmic. Partially membrane-associated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=SHAG1a, ASAP1a;
CC IsoId=Q9QWY8-1; Sequence=Displayed;
CC Name=2; Synonyms=SHAG1b, ASAP1b;
CC IsoId=Q9QWY8-2; Sequence=VSP_008368;
CC Name=3;
CC IsoId=Q9QWY8-3; Sequence=VSP_008366;
CC Name=4;
CC IsoId=Q9QWY8-4; Sequence=VSP_008367;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined but a most
CC abundant expression was found in the testis, brain, lung and spleen. A
CC heightened expression was seen in the adipose tissue from obese (ob)
CC and diabetic (db) animals. {ECO:0000269|PubMed:10022919}.
CC -!- DOMAIN: The PH domain most probably contributes to the
CC phosphoinositide-dependent regulation of ADP ribosylation factors.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC.
CC {ECO:0000269|PubMed:12771146}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH48818.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF075461; AAC98349.1; -; mRNA.
DR EMBL; AF075462; AAC98350.1; -; mRNA.
DR EMBL; AC098728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002201; AAH02201.1; ALT_INIT; mRNA.
DR EMBL; BC048818; AAH48818.1; ALT_INIT; mRNA.
DR EMBL; BC094581; AAH94581.1; -; mRNA.
DR EMBL; AK122477; BAC65759.1; -; mRNA.
DR EMBL; U92478; AAB82338.1; -; mRNA.
DR CCDS; CCDS56986.1; -. [Q9QWY8-1]
DR CCDS; CCDS70634.1; -. [Q9QWY8-2]
DR PIR; T42627; T42627.
DR RefSeq; NP_001263390.1; NM_001276461.1.
DR RefSeq; NP_001263391.1; NM_001276462.1.
DR RefSeq; NP_001263396.1; NM_001276467.1. [Q9QWY8-2]
DR RefSeq; NP_034156.2; NM_010026.3. [Q9QWY8-1]
DR PDB; 5C6R; X-ray; 1.80 A; A/B=325-451.
DR PDB; 5C79; X-ray; 1.60 A; A/B=325-451.
DR PDBsum; 5C6R; -.
DR PDBsum; 5C79; -.
DR AlphaFoldDB; Q9QWY8; -.
DR BMRB; Q9QWY8; -.
DR SMR; Q9QWY8; -.
DR BioGRID; 199076; 47.
DR IntAct; Q9QWY8; 9.
DR MINT; Q9QWY8; -.
DR STRING; 10090.ENSMUSP00000134825; -.
DR iPTMnet; Q9QWY8; -.
DR PhosphoSitePlus; Q9QWY8; -.
DR EPD; Q9QWY8; -.
DR jPOST; Q9QWY8; -.
DR MaxQB; Q9QWY8; -.
DR PaxDb; Q9QWY8; -.
DR PRIDE; Q9QWY8; -.
DR ProteomicsDB; 281910; -. [Q9QWY8-1]
DR ProteomicsDB; 281911; -. [Q9QWY8-2]
DR ProteomicsDB; 281912; -. [Q9QWY8-3]
DR ProteomicsDB; 281913; -. [Q9QWY8-4]
DR Antibodypedia; 27290; 244 antibodies from 30 providers.
DR DNASU; 13196; -.
DR Ensembl; ENSMUST00000110115; ENSMUSP00000105742; ENSMUSG00000022377. [Q9QWY8-4]
DR Ensembl; ENSMUST00000175793; ENSMUSP00000135718; ENSMUSG00000022377. [Q9QWY8-3]
DR Ensembl; ENSMUST00000176384; ENSMUSP00000135190; ENSMUSG00000022377. [Q9QWY8-2]
DR Ensembl; ENSMUST00000177374; ENSMUSP00000134825; ENSMUSG00000022377. [Q9QWY8-1]
DR GeneID; 13196; -.
DR KEGG; mmu:13196; -.
DR UCSC; uc007vzh.2; mouse. [Q9QWY8-3]
DR UCSC; uc007vzk.2; mouse. [Q9QWY8-1]
DR UCSC; uc007vzl.2; mouse. [Q9QWY8-2]
DR CTD; 50807; -.
DR MGI; MGI:1342335; Asap1.
DR VEuPathDB; HostDB:ENSMUSG00000022377; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000158547; -.
DR InParanoid; Q9QWY8; -.
DR OMA; CAVKNGM; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q9QWY8; -.
DR TreeFam; TF325156; -.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 13196; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Asap1; mouse.
DR PRO; PR:Q9QWY8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QWY8; protein.
DR Bgee; ENSMUSG00000022377; Expressed in saccule of membranous labyrinth and 254 other tissues.
DR ExpressionAtlas; Q9QWY8; baseline and differential.
DR Genevisible; Q9QWY8; MM.
DR GO; GO:0031253; C:cell projection membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0002102; C:podosome; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:FlyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IDA:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; IDA:MGI.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IBA:GO_Central.
DR CDD; cd07641; BAR_ASAP1; 1.
DR CDD; cd13251; PH_ASAP; 1.
DR CDD; cd11965; SH3_ASAP1; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 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; 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; PTHR45854; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 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; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF57863; SSF57863; 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.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat;
KW Cilium biogenesis/degradation; Cytoplasm; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Zinc; Zinc-finger.
FT CHAIN 1..1147
FT /note="Arf-GAP with SH3 domain, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000074197"
FT DOMAIN 339..431
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 454..577
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 615..647
FT /note="ANK 1"
FT REPEAT 651..680
FT /note="ANK 2"
FT DOMAIN 1085..1147
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 469..492
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000269|PubMed:12771146"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1AAU6"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULH1"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1066
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 304..318
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008367"
FT VAR_SEQ 304..315
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_008366"
FT VAR_SEQ 816..872
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9819391"
FT /id="VSP_008368"
FT MUTAGEN 811
FT /note="R->A: Significant reduction in binding to SRC and
FT CRK and loss of phosphorylation. Loss of binding and
FT phosphorylation; when associated with A-910 and A-913."
FT /evidence="ECO:0000269|PubMed:9819391"
FT MUTAGEN 910
FT /note="P->A: Significant reduction in binding to SRC and
FT CRK and decrease in phosphorylation; when associated with
FT A-913. Loss of binding and phosphorylation; when associated
FT with A-811 and A-913."
FT /evidence="ECO:0000269|PubMed:9819391"
FT MUTAGEN 913
FT /note="P->A: Significant reduction in binding to SRC and
FT CRK and decrease in phosphorylation; when associated with
FT A-910. Loss of binding and phosphorylation; when associated
FT with A-811 and A-910."
FT /evidence="ECO:0000269|PubMed:9819391"
FT CONFLICT 654
FT /note="T -> S (in Ref. 5; AAB82338)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="L -> S (in Ref. 1; AAC98349/AAC98350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="R -> I (in Ref. 5; AAB82338)"
FT /evidence="ECO:0000305"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5C6R"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5C6R"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5C79"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 394..404
FT /evidence="ECO:0007829|PDB:5C79"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:5C79"
FT HELIX 416..436
FT /evidence="ECO:0007829|PDB:5C79"
SQ SEQUENCE 1147 AA; 127421 MW; 12950D1C4F49A909 CRC64;
MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL
EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK
FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI
EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL
IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
PKEVGGLYVA SRANSSRRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS DGIRKVWQRR
KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF DLISHNRTYH FQAEDEQDYI
AWISVLTNSK EEALTMAFRG EQSTGENSLE DLTKAIIEDV QRLPGNDICC DCGSSEPTWL
STNLGILTCI ECSGIHREMG VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS
PSPKPTPSSD MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE
GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS VGNTVLHYCS
MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC EDLLSQAKSG KFNPHVHVEY
EWNLRQDEMD ESDDDLDDKP SPIKKERSPR PQSFCHSSSI SPQDKLALPG FSTPRDKQRL
SYGAFTNQIF ASTSTDLPTS PTSEAPPLPP RNAGKGPTGP PSTLPLGTQT SSGSSTLSKK
RPPPPPPGHK RTLSDPPSPL PHGPPNKGAI PWGNDVGPLS SSKTANKFEG LSQQASTSSA
KTALGPRVLP KLPQKVALRK TETSHHLSLD RTNIPPETFQ KSSQLTELPQ KPPLGELPPK
PVELAPKPQV GELPPKPGEL PPKPQLGDLP PKPQLSDLPP KPQMKDLPPK PQLGDLLAKS
QAGDVSAKVQ PPSEVTQRSH TGDLSPNVQS RDAIQKQASE DSNDLTPTLP ETPVPLPRKI
NTGKNKVRRV KTIYDCQADN DDELTFIEGE VIIVTGEEDQ EWWIGHIEGQ PERKGVFPVS
FVHILSD
