VAT1_HUMAN
ID VAT1_HUMAN Reviewed; 393 AA.
AC Q99536; A8K345; B0AZP7; B4DPX4; Q13035; Q5BKZ7; Q96A39; Q9BUT8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog;
DE EC=1.-.-.-;
GN Name=VAT1;
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 [GENOMIC DNA].
RX PubMed=8938427; DOI=10.1101/gr.6.11.1029;
RA Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L.,
RA King M.-C.;
RT "Complete genomic sequence and analysis of 117 kb of human DNA containing
RT the gene BRCA1.";
RL Genome Res. 6:1029-1049(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain;
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Ovary, Skin, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-61; 64-82; 85-96; 103-128; 211-225; 256-271; 282-295
RP AND 322-344, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-393 (ISOFORM 1).
RX PubMed=7774926; DOI=10.1016/0888-7543(95)80133-7;
RA Friedman L.S., Ostermeyer E.A., Lynch E.D., Szabo C.I., Meza J.E.,
RA Anderson L.A., Dowd P., Lee M.K., Rowell S.E., Ellison J., Boyd J.,
RA King M.-C.;
RT "22 genes from chromosome 17q21: cloning, sequencing, and characterization
RT of mutations in breast cancer families and tumors.";
RL Genomics 25:256-263(1995).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12898150; DOI=10.1007/s00403-003-0421-8;
RA Koch J., Foekens J., Timmermans M., Fink W., Wirzbach A., Kramer M.D.,
RA Schaefer B.M.;
RT "Human VAT-1: a calcium-regulated activation marker of human epithelial
RT cells.";
RL Arch. Dermatol. Res. 295:203-210(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MFN1 AND MFN2.
RX PubMed=17105775; DOI=10.1242/jcs.03253;
RA Eura Y., Ishihara N., Oka T., Mihara K.;
RT "Identification of a novel protein that regulates mitochondrial fusion by
RT modulating mitofusin (Mfn) protein function.";
RL J. Cell Sci. 119:4913-4925(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY
RP WOUNDING.
RX PubMed=19508442; DOI=10.1111/j.1365-2990.2009.00993.x;
RA Mertsch S., Becker M., Lichota A., Paulus W., Senner V.;
RT "Vesicle amine transport protein-1 (VAT-1) is upregulated in glioblastomas
RT and promotes migration.";
RL Neuropathol. Appl. Neurobiol. 35:342-352(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-27; SER-35 AND
RP SER-44, AND 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).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Possesses ATPase activity (By similarity). Plays a part in
CC calcium-regulated keratinocyte activation in epidermal repair
CC mechanisms. Has no effect on cell proliferation. Negatively regulates
CC mitochondrial fusion in cooperation with mitofusin proteins (MFN1-2).
CC {ECO:0000250, ECO:0000269|PubMed:12898150, ECO:0000269|PubMed:17105775,
CC ECO:0000269|PubMed:19508442}.
CC -!- INTERACTION:
CC Q99536; P60201-2: PLP1; NbExp=3; IntAct=EBI-2514883, EBI-12188331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion outer membrane;
CC Peripheral membrane protein. Note=The majority is localized in the
CC cytoplasm and a small amount is associated with mitochondria.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99536-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99536-2; Sequence=VSP_055794;
CC Name=3;
CC IsoId=Q99536-3; Sequence=VSP_055795;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Also expressed in glioblastoma
CC cells. {ECO:0000269|PubMed:19508442}.
CC -!- INDUCTION: Increased expression in glioblastomas and on wounding, in
CC basal keratinocytes. This expression is calcium ion-dependent.
CC {ECO:0000269|PubMed:19508442}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37596.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L78833; AAC37596.1; ALT_INIT; Genomic_DNA.
DR EMBL; BT007369; AAP36033.1; -; mRNA.
DR EMBL; AK298536; BAG60736.1; -; mRNA.
DR EMBL; AK290460; BAF83149.1; -; mRNA.
DR EMBL; AK315838; BAF98729.1; -; mRNA.
DR EMBL; AC055866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60917.1; -; Genomic_DNA.
DR EMBL; BC001913; AAH01913.2; -; mRNA.
DR EMBL; BC008725; AAH08725.2; -; mRNA.
DR EMBL; BC014279; AAH14279.1; -; mRNA.
DR EMBL; BC015041; AAH15041.1; -; mRNA.
DR EMBL; BC090858; AAH90858.1; -; mRNA.
DR EMBL; U18009; AAA95990.1; -; mRNA.
DR CCDS; CCDS11451.1; -. [Q99536-1]
DR RefSeq; NP_006364.2; NM_006373.3. [Q99536-1]
DR PDB; 6K9Y; X-ray; 2.20 A; A/B/C/D=41-393.
DR PDB; 6LHR; X-ray; 2.62 A; A/B/C/D=43-393.
DR PDB; 6LII; X-ray; 2.30 A; A/B/C/D=43-393.
DR PDBsum; 6K9Y; -.
DR PDBsum; 6LHR; -.
DR PDBsum; 6LII; -.
DR AlphaFoldDB; Q99536; -.
DR SMR; Q99536; -.
DR BioGRID; 115756; 72.
DR IntAct; Q99536; 22.
DR MINT; Q99536; -.
DR STRING; 9606.ENSP00000347872; -.
DR BindingDB; Q99536; -.
DR ChEMBL; CHEMBL4802015; -.
DR GlyGen; Q99536; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99536; -.
DR MetOSite; Q99536; -.
DR PhosphoSitePlus; Q99536; -.
DR SwissPalm; Q99536; -.
DR BioMuta; VAT1; -.
DR DMDM; 52788294; -.
DR EPD; Q99536; -.
DR jPOST; Q99536; -.
DR MassIVE; Q99536; -.
DR MaxQB; Q99536; -.
DR PaxDb; Q99536; -.
DR PeptideAtlas; Q99536; -.
DR PRIDE; Q99536; -.
DR ProteomicsDB; 2531; -.
DR ProteomicsDB; 78312; -. [Q99536-1]
DR TopDownProteomics; Q99536-1; -. [Q99536-1]
DR Antibodypedia; 29494; 90 antibodies from 25 providers.
DR DNASU; 10493; -.
DR Ensembl; ENST00000355653.8; ENSP00000347872.2; ENSG00000108828.16. [Q99536-1]
DR Ensembl; ENST00000420567.7; ENSP00000408553.2; ENSG00000108828.16. [Q99536-2]
DR Ensembl; ENST00000587173.5; ENSP00000465946.1; ENSG00000108828.16. [Q99536-3]
DR GeneID; 10493; -.
DR KEGG; hsa:10493; -.
DR MANE-Select; ENST00000355653.8; ENSP00000347872.2; NM_006373.4; NP_006364.2.
DR UCSC; uc002icm.2; human. [Q99536-1]
DR CTD; 10493; -.
DR DisGeNET; 10493; -.
DR GeneCards; VAT1; -.
DR HGNC; HGNC:16919; VAT1.
DR HPA; ENSG00000108828; Low tissue specificity.
DR MIM; 604631; gene.
DR neXtProt; NX_Q99536; -.
DR OpenTargets; ENSG00000108828; -.
DR VEuPathDB; HostDB:ENSG00000108828; -.
DR eggNOG; KOG1197; Eukaryota.
DR GeneTree; ENSGT00940000157579; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; Q99536; -.
DR OMA; ACAINRH; -.
DR PhylomeDB; Q99536; -.
DR TreeFam; TF314255; -.
DR PathwayCommons; Q99536; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q99536; -.
DR BioGRID-ORCS; 10493; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; VAT1; human.
DR GeneWiki; VAT1; -.
DR GenomeRNAi; 10493; -.
DR Pharos; Q99536; Tbio.
DR PRO; PR:Q99536; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99536; protein.
DR Bgee; ENSG00000108828; Expressed in right adrenal gland cortex and 204 other tissues.
DR ExpressionAtlas; Q99536; baseline and differential.
DR Genevisible; Q99536; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:UniProtKB.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330"
FT CHAIN 2..393
FT /note="Synaptic vesicle membrane protein VAT-1 homolog"
FT /id="PRO_0000160918"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MIE4"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055794"
FT VAR_SEQ 61..128
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055795"
FT CONFLICT 71
FT /note="P -> A (in Ref. 1; AAC37596)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..86
FT /note="RLRAC -> NSARG (in Ref. 8; AAA95990)"
FT /evidence="ECO:0000305"
FT CONFLICT 207..208
FT /note="QL -> HV (in Ref. 8; AAA95990)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="E -> Q (in Ref. 1; AAC37596)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="N -> S (in Ref. 8; AAA95990)"
FT /evidence="ECO:0000305"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:6K9Y"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6K9Y"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6LHR"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6K9Y"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6LHR"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6K9Y"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:6LII"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6K9Y"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:6K9Y"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:6K9Y"
SQ SEQUENCE 393 AA; 41920 MW; 25933347742C2FE6 CRC64;
MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD
KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA
VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL
FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY
HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA
LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS
VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN
