ID   VEZA_HUMAN              Reviewed;         779 AA.
AC   Q9HBM0; Q6P1Q3; Q9H2F4; Q9H2U5; Q9NT70; Q9NVW0; Q9UF91;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Vezatin;
GN   Name=VEZT;
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] (ISOFORM 1), AND VARIANT ASP-762.
RC   TISSUE=Adrenal gland;
RA   Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.;
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT, AND VARIANT ILE-496.
RC   TISSUE=Retina;
RX   PubMed=11080149; DOI=10.1093/emboj/19.22.6020;
RA   Kuessel-Andermann P., El-Amraoui A., Safieddine S., Nouaille S.,
RA   Perfettini I., Lecuit M., Cossart P., Wolfrum U., Petit C.;
RT   "Vezatin, a novel transmembrane protein, bridges myosin VIIA to the
RT   cadherin-catenins complex.";
RL   EMBO J. 19:6020-6029(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Skin;
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 MRNA] OF 1-610 (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 391-779 (ISOFORM 1), AND VARIANTS MET-612
RP   AND ASP-762.
RC   TISSUE=Amygdala, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX   PubMed=15090598; DOI=10.1242/jcs.01066;
RA   Sousa S., Cabanes D., El-Amraoui A., Petit C., Lecuit M., Cossart P.;
RT   "Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria
RT   entry into epithelial cells.";
RL   J. Cell Sci. 117:2121-2130(2004).
CC   -!- FUNCTION: Plays a pivotal role in the establishment of adherens
CC       junctions and their maintenance in adult life. Required for
CC       morphogenesis of the preimplantation embryo, and for the implantation
CC       process. {ECO:0000250|UniProtKB:Q3ZK22}.
CC   -!- FUNCTION: (Microbial infection) In case of Listeria infection, promotes
CC       bacterial internalization by participating in myosin VIIa recruitment
CC       to the entry site. {ECO:0000269|PubMed:15090598}.
CC   -!- SUBUNIT: Interacts with USH2A (via the cytoplasmic region); the
CC       interaction associates VEZT with the USH2 complex at the stereocilia
CC       base (By similarity). Interacts with myosin MYO7A and the cadherin-
CC       catenins complex (PubMed:11080149). {ECO:0000250|UniProtKB:Q3ZK22,
CC       ECO:0000269|PubMed:11080149}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15090598};
CC       Multi-pass membrane protein {ECO:0000305}. Cell projection,
CC       stereocilium membrane {ECO:0000250|UniProtKB:Q3ZK22}. Cell junction,
CC       adherens junction {ECO:0000269|PubMed:15090598}. Nucleus
CC       {ECO:0000250|UniProtKB:Q3ZK22}. Cytoplasmic vesicle, secretory vesicle,
CC       acrosome {ECO:0000250|UniProtKB:Q3ZK22}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q9HBM0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HBM0-2; Sequence=VSP_004010, VSP_004011, VSP_004014,
CC                                  VSP_004017;
CC       Name=5;
CC         IsoId=Q9HBM0-5; Sequence=VSP_040854, VSP_040855;
CC       Name=6;
CC         IsoId=Q9HBM0-6; Sequence=VSP_040853, VSP_040856;
CC   -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the vezatin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG38514.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC       Sequence=AAH64939.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=BAA91634.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=CAB70772.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF225417; AAG09719.1; -; mRNA.
DR   EMBL; AF216644; AAG38485.1; -; mRNA.
DR   EMBL; AF277625; AAG38514.1; ALT_SEQ; mRNA.
DR   EMBL; AK001338; BAA91634.1; ALT_SEQ; mRNA.
DR   EMBL; AC084879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064939; AAH64939.1; ALT_SEQ; mRNA.
DR   EMBL; AL133113; CAB61416.1; -; mRNA.
DR   EMBL; AL137497; CAB70772.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS44954.1; -. [Q9HBM0-1]
DR   PIR; T46251; T46251.
DR   RefSeq; NP_060069.3; NM_017599.3. [Q9HBM0-1]
DR   RefSeq; XP_006719553.1; XM_006719490.3.
DR   RefSeq; XP_016875091.1; XM_017019602.1.
DR   AlphaFoldDB; Q9HBM0; -.
DR   SMR; Q9HBM0; -.
DR   BioGRID; 120736; 196.
DR   IntAct; Q9HBM0; 38.
DR   MINT; Q9HBM0; -.
DR   STRING; 9606.ENSP00000410083; -.
DR   TCDB; 8.A.134.1.1; the vezatin (vezatin) family.
DR   iPTMnet; Q9HBM0; -.
DR   PhosphoSitePlus; Q9HBM0; -.
DR   SwissPalm; Q9HBM0; -.
DR   BioMuta; VEZT; -.
DR   DMDM; 224471870; -.
DR   EPD; Q9HBM0; -.
DR   jPOST; Q9HBM0; -.
DR   MassIVE; Q9HBM0; -.
DR   MaxQB; Q9HBM0; -.
DR   PaxDb; 9606-ENSP00000410083; -.
DR   PeptideAtlas; Q9HBM0; -.
DR   ProteomicsDB; 81573; -. [Q9HBM0-1]
DR   ProteomicsDB; 81574; -. [Q9HBM0-2]
DR   ProteomicsDB; 81575; -. [Q9HBM0-5]
DR   ProteomicsDB; 81576; -. [Q9HBM0-6]
DR   Pumba; Q9HBM0; -.
DR   Antibodypedia; 1345; 73 antibodies from 23 providers.
DR   DNASU; 55591; -.
DR   Ensembl; ENST00000436874.6; ENSP00000410083.1; ENSG00000028203.19. [Q9HBM0-1]
DR   Ensembl; ENST00000546557.5; ENSP00000447080.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000547484.5; ENSP00000447010.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000547997.5; ENSP00000449346.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000548455.5; ENSP00000447044.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000549624.5; ENSP00000448555.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000550803.5; ENSP00000449056.1; ENSG00000028203.19. [Q9HBM0-6]
DR   Ensembl; ENST00000552660.5; ENSP00000447786.1; ENSG00000028203.19. [Q9HBM0-6]
DR   GeneID; 55591; -.
DR   KEGG; hsa:55591; -.
DR   MANE-Select; ENST00000436874.6; ENSP00000410083.1; NM_017599.4; NP_060069.3.
DR   UCSC; uc001tdz.2; human. [Q9HBM0-1]
DR   AGR; HGNC:18258; -.
DR   CTD; 55591; -.
DR   DisGeNET; 55591; -.
DR   GeneCards; VEZT; -.
DR   HGNC; HGNC:18258; VEZT.
DR   HPA; ENSG00000028203; Low tissue specificity.
DR   MIM; 619749; gene.
DR   neXtProt; NX_Q9HBM0; -.
DR   OpenTargets; ENSG00000028203; -.
DR   PharmGKB; PA143485667; -.
DR   VEuPathDB; HostDB:ENSG00000028203; -.
DR   eggNOG; ENOG502QTQW; Eukaryota.
DR   GeneTree; ENSGT00390000003290; -.
DR   InParanoid; Q9HBM0; -.
DR   OMA; IVCENPR; -.
DR   OrthoDB; 3026684at2759; -.
DR   PhylomeDB; Q9HBM0; -.
DR   TreeFam; TF332269; -.
DR   PathwayCommons; Q9HBM0; -.
DR   SignaLink; Q9HBM0; -.
DR   BioGRID-ORCS; 55591; 354 hits in 1160 CRISPR screens.
DR   ChiTaRS; VEZT; human.
DR   GeneWiki; VEZT; -.
DR   GenomeRNAi; 55591; -.
DR   Pharos; Q9HBM0; Tbio.
DR   PRO; PR:Q9HBM0; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9HBM0; Protein.
DR   Bgee; ENSG00000028203; Expressed in adrenal tissue and 192 other cell types or tissues.
DR   ExpressionAtlas; Q9HBM0; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR   GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   InterPro; IPR026859; Myosin-bd.
DR   InterPro; IPR026858; Vezatin.
DR   PANTHER; PTHR15989; VEZATIN; 1.
DR   PANTHER; PTHR15989:SF5; VEZATIN; 1.
DR   Pfam; PF12632; Vezatin; 1.
DR   Genevisible; Q9HBM0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Coiled coil; Cytoplasmic vesicle; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..779
FT                   /note="Vezatin"
FT                   /id="PRO_0000065783"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          618..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..462
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        621..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..48
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11080149,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_004010"
FT   VAR_SEQ         49..55
FT                   /note="PPTRVLP -> MLKEWAI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11080149,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_004011"
FT   VAR_SEQ         57..79
FT                   /note="QGILLKVAETIKSWIFFSQCNKK -> YLGYSNHSMNINCTYWHAQGMGY
FT                   (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040853"
FT   VAR_SEQ         57..65
FT                   /note="QGILLKVAE -> GSLSAICLH (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040854"
FT   VAR_SEQ         66..779
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040855"
FT   VAR_SEQ         80..779
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040856"
FT   VAR_SEQ         611..617
FT                   /note="AVLKSLS -> GVKSAWN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11080149,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_004014"
FT   VAR_SEQ         618..779
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11080149,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_004017"
FT   VARIANT         162
FT                   /note="T -> A (in dbSNP:rs17855933)"
FT                   /id="VAR_046303"
FT   VARIANT         496
FT                   /note="V -> I (in dbSNP:rs10507051)"
FT                   /evidence="ECO:0000269|PubMed:11080149"
FT                   /id="VAR_046304"
FT   VARIANT         612
FT                   /note="V -> M (in dbSNP:rs17344738)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_046305"
FT   VARIANT         668
FT                   /note="S -> A (in dbSNP:rs17855934)"
FT                   /id="VAR_046306"
FT   VARIANT         762
FT                   /note="G -> D (in dbSNP:rs14121)"
FT                   /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1"
FT                   /id="VAR_014945"
FT   CONFLICT        46
FT                   /note="Q -> R (in Ref. 3; BAA91634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="W -> R (in Ref. 2; AAG38485)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="L -> W (in Ref. 1; AAG09719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="Y -> I (in Ref. 1; AAG09719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="S -> T (in Ref. 1; AAG09719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        617
FT                   /note="S -> F (in Ref. 1; AAG09719)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   779 AA;  88665 MW;  4B59BBAA491A71A5 CRC64;
     MTPEFDEEVV FENSPLYQYL QDLGHTDFEI CSSLSPKTEK CTTEGQQKPP TRVLPKQGIL
     LKVAETIKSW IFFSQCNKKD DLLHKLDIGF RLDSLHTILQ QEVLLQEDVE LIELLDPSIL
     SAGQSQQQEN GHLPTLCSLA TPNIWDLSML FAFISLLVML PTWWIVSSWL VWGVILFVYL
     VIRALRLWRT AKLQVTLKKY SVHLEDMATN SRAFTNLVRK ALRLIQETEV ISRGFTLVSA
     ACPFNKAGQH PSQHLIGLRK AVYRTLRANF QAARLATLYM LKNYPLNSES DNVTNYICVV
     PFKELGLGLS EEQISEEEAH NFTDGFSLPA LKVLFQLWVA QSSEFFRRLA LLLSTANSPP
     GPLLTPALLP HRILSDVTQG LPHAHSACLE ELKRSYEFYR YFETQHQSVP QCLSKTQQKS
     RELNNVHTAV RSLQLHLKAL LNEVIILEDE LEKLVCTKET QELVSEAYPI LEQKLKLIQP
     HVQASNNCWE EAISQVDKLL RRNTDKKGKP EIACENPHCT VVPLKQPTLH IADKDPIPEE
     QELEAYVDDI DIDSDFRKDD FYYLSQEDKE RQKREHEESK RVLQELKSVL GFKASEAERQ
     KWKQLLFSDH AVLKSLSPVD PVEPISNSEP SMNSDMGKVS KNDTEEESNK SATTDNEISR
     TEYLCENSLE GKNKDNSSNE VFPQGAEERM CYQCESEDEP QADGSGLTTA PPTPRDSLQP
     SIKQRLARLQ LSPDFTFTAG LAAEVAARSL SFTTMQEQTF GGEEEEQIIE ENKNEIEEK
//