ID   ACAP2_HUMAN             Reviewed;         778 AA.
AC   Q15057; A8K2V4; Q8N5Z8; Q9UQR3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 3.
DT   24-JAN-2024, entry version 213.
DE   RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE   AltName: Full=Centaurin-beta-2;
DE            Short=Cnt-b2;
GN   Name=ACAP2; Synonyms=CENTB2, KIAA0041;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF ARG-442.
RC   TISSUE=Leukocyte;
RX   PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA   Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W.,
RA   Donaldson J.G., Randazzo P.A.;
RT   "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT   periphery.";
RL   J. Cell Biol. 151:627-638(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA   Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA   Kawarabayasi Y., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. II. The
RT   coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 1:223-229(1994).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Nomura N.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-581 AND SER-775, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC       (ARF6). {ECO:0000269|PubMed:11062263}.
CC   -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC       4,5-bisphosphate (PIP2) and phosphatidic acid.
CC       {ECO:0000269|PubMed:11062263}.
CC   -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC       direct and probably recruits ACAP2 to membranes. Interacts with
CC       MICALL1; the interaction is indirect through RAB35 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest level in lung.
CC       {ECO:0000269|PubMed:11062263}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05064.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB41450.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ238248; CAB41450.1; ALT_FRAME; mRNA.
DR   EMBL; D26069; BAA05064.2; ALT_INIT; mRNA.
DR   EMBL; AK290369; BAF83058.1; -; mRNA.
DR   EMBL; CH471052; EAW78027.1; -; Genomic_DNA.
DR   EMBL; BC031005; AAH31005.1; -; mRNA.
DR   EMBL; BC060767; AAH60767.1; -; mRNA.
DR   CCDS; CCDS33924.1; -.
DR   RefSeq; NP_036419.3; NM_012287.5.
DR   PDB; 6IF3; X-ray; 1.50 A; A=601-770.
DR   PDBsum; 6IF3; -.
DR   AlphaFoldDB; Q15057; -.
DR   SMR; Q15057; -.
DR   BioGRID; 117073; 49.
DR   IntAct; Q15057; 14.
DR   MINT; Q15057; -.
DR   STRING; 9606.ENSP00000324287; -.
DR   GlyCosmos; Q15057; 1 site, 1 glycan.
DR   GlyGen; Q15057; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q15057; -.
DR   MetOSite; Q15057; -.
DR   PhosphoSitePlus; Q15057; -.
DR   BioMuta; ACAP2; -.
DR   DMDM; 39932727; -.
DR   EPD; Q15057; -.
DR   jPOST; Q15057; -.
DR   MassIVE; Q15057; -.
DR   MaxQB; Q15057; -.
DR   PaxDb; 9606-ENSP00000324287; -.
DR   PeptideAtlas; Q15057; -.
DR   ProteomicsDB; 60412; -.
DR   Pumba; Q15057; -.
DR   Antibodypedia; 19460; 238 antibodies from 36 providers.
DR   DNASU; 23527; -.
DR   Ensembl; ENST00000326793.11; ENSP00000324287.6; ENSG00000114331.16.
DR   GeneID; 23527; -.
DR   KEGG; hsa:23527; -.
DR   MANE-Select; ENST00000326793.11; ENSP00000324287.6; NM_012287.6; NP_036419.3.
DR   UCSC; uc003fun.5; human.
DR   AGR; HGNC:16469; -.
DR   CTD; 23527; -.
DR   DisGeNET; 23527; -.
DR   GeneCards; ACAP2; -.
DR   HGNC; HGNC:16469; ACAP2.
DR   HPA; ENSG00000114331; Low tissue specificity.
DR   MIM; 607766; gene.
DR   neXtProt; NX_Q15057; -.
DR   OpenTargets; ENSG00000114331; -.
DR   PharmGKB; PA26407; -.
DR   VEuPathDB; HostDB:ENSG00000114331; -.
DR   eggNOG; KOG0521; Eukaryota.
DR   GeneTree; ENSGT00940000156389; -.
DR   HOGENOM; CLU_012513_0_1_1; -.
DR   InParanoid; Q15057; -.
DR   OMA; DWEPEIL; -.
DR   OrthoDB; 1449795at2759; -.
DR   PhylomeDB; Q15057; -.
DR   TreeFam; TF318315; -.
DR   PathwayCommons; Q15057; -.
DR   SignaLink; Q15057; -.
DR   BioGRID-ORCS; 23527; 47 hits in 1157 CRISPR screens.
DR   ChiTaRS; ACAP2; human.
DR   GeneWiki; CENTB2; -.
DR   GenomeRNAi; 23527; -.
DR   Pharos; Q15057; Tbio.
DR   PRO; PR:Q15057; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q15057; Protein.
DR   Bgee; ENSG00000114331; Expressed in epithelium of nasopharynx and 203 other cell types or tissues.
DR   ExpressionAtlas; Q15057; baseline and differential.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030029; P:actin filament-based process; IDA:MGI.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   CDD; cd08851; ArfGap_ACAP2; 1.
DR   CDD; cd07638; BAR_ACAP2; 1.
DR   CDD; cd13250; PH_ACAP; 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; IPR045258; ACAP1/2/3-like.
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; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23180:SF241; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR23180; CENTAURIN/ARF; 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.
DR   Genevisible; Q15057; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Coiled coil; Endosome; GTPase activation;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..778
FT                   /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT                   containing protein 2"
FT                   /id="PRO_0000074210"
FT   DOMAIN          1..226
FT                   /note="BAR"
FT   DOMAIN          266..361
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          399..520
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REPEAT          640..669
FT                   /note="ANK 1"
FT   REPEAT          673..702
FT                   /note="ANK 2"
FT   REPEAT          706..735
FT                   /note="ANK 3"
FT   ZN_FING         414..437
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          371..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT   MOD_RES         742
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MUTAGEN         442
FT                   /note="R->Q: Loss of GAP activity."
FT                   /evidence="ECO:0000269|PubMed:11062263"
FT   CONFLICT        5
FT                   /note="V -> G (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="C -> G (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="V -> G (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="S -> R (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="E -> K (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="L -> V (in Ref. 1; CAB41450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        564
FT                   /note="G -> E (in Ref. 6; AAH60767)"
FT                   /evidence="ECO:0000305"
FT   HELIX           606..615
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           619..627
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   TURN            637..641
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           644..651
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           654..662
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           677..684
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           687..695
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           710..716
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           720..737
FT                   /evidence="ECO:0007829|PDB:6IF3"
FT   HELIX           753..757
FT                   /evidence="ECO:0007829|PDB:6IF3"
SQ   SEQUENCE   778 AA;  88029 MW;  64B620957FEE6195 CRC64;
     MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
     NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
     KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
     QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
     KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
     KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
     ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA
     DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
     ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS
     ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD
     SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL
     LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA
     DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF
//