VEZA_HUMAN
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 03-AUG-2022, entry version 159.
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};
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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. [Q9HBM0-2]
DR AlphaFoldDB; Q9HBM0; -.
DR SMR; Q9HBM0; -.
DR BioGRID; 120736; 176.
DR IntAct; Q9HBM0; 28.
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 BioMuta; VEZT; -.
DR DMDM; 224471870; -.
DR EPD; Q9HBM0; -.
DR jPOST; Q9HBM0; -.
DR MassIVE; Q9HBM0; -.
DR MaxQB; Q9HBM0; -.
DR PaxDb; Q9HBM0; -.
DR PeptideAtlas; Q9HBM0; -.
DR PRIDE; Q9HBM0; -.
DR ProteomicsDB; 81573; -. [Q9HBM0-1]
DR ProteomicsDB; 81574; -. [Q9HBM0-2]
DR ProteomicsDB; 81575; -. [Q9HBM0-5]
DR ProteomicsDB; 81576; -. [Q9HBM0-6]
DR Antibodypedia; 1345; 64 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 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; 1379096at2759; -.
DR PhylomeDB; Q9HBM0; -.
DR TreeFam; TF332269; -.
DR PathwayCommons; Q9HBM0; -.
DR SignaLink; Q9HBM0; -.
DR BioGRID-ORCS; 55591; 349 hits in 1085 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 190 other tissues.
DR ExpressionAtlas; Q9HBM0; baseline and differential.
DR Genevisible; Q9HBM0; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR15989; 1.
DR Pfam; PF12632; Vezatin; 1.
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
