ID VPP2_HUMAN Reviewed; 856 AA. AC Q9Y487; A8K026; Q6NUM0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=V-type proton ATPase 116 kDa subunit a 2; DE Short=V-ATPase 116 kDa subunit a 2; DE AltName: Full=Lysosomal H(+)-transporting ATPase V0 subunit a 2; DE AltName: Full=TJ6; DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2; GN Name=ATP6V0A2; 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]. RA Babichev Y., Isakov N.; RT "Characterization of human TJ6 homolog."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Astrocyte; 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 [5] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSCD2. RX PubMed=16415858; DOI=10.1038/ncb1348; RA Hurtado-Lorenzo A., Skinner M., El Annan J., Futai M., Sun-Wada G.-H., RA Bourgoin S., Casanova J., Wildeman A., Bechoua S., Ausiello D.A., Brown D., RA Marshansky V.; RT "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the RT protein degradative pathway."; RL Nat. Cell Biol. 8:124-136(2006). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=17295899; DOI=10.1111/j.1600-0897.2006.00463.x; RA Ntrivalas E., Gilman-Sachs A., Kwak-Kim J., Beaman K.; RT "The N-terminal domain of the a2 isoform of vacuolar ATPase can regulate RT interleukin-1beta production from mononuclear cells in co-culture with JEG- RT 3 choriocarcinoma cells."; RL Am. J. Reprod. Immunol. 57:201-209(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] RP INVOLVEMENT IN ARCL2A, INVOLVEMENT IN WSS, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=18157129; DOI=10.1038/ng.2007.45; RA Kornak U., Reynders E., Dimopoulou A., van Reeuwijk J., Fischer B., RA Rajab A., Budde B., Nuernberg P., Foulquier F., Dobyns W.B., Quelhas D., RA Vilarinho L., Leao-Teles E., Greally M., Seemanova E., Simandlova M., RA Salih M., Nanda A., Basel-Vanagaite L., Kayserili H., Yuksel-Apak M., RA Larregue M., Vigneron J., Giurgea S., Lefeber D., Urban Z., Gruenewald S., RA Annaert W., Brunner H.G., van Bokhoven H., Wevers R., Morava E., RA Matthijs G., Van Maldergem L., Mundlos S.; RT "Impaired glycosylation and cutis laxa caused by mutations in the vesicular RT H+-ATPase subunit ATP6V0A2."; RL Nat. Genet. 40:32-34(2008). RN [9] 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [12] RP FUNCTION. RX PubMed=28296633; DOI=10.7554/elife.22693; RA Miles A.L., Burr S.P., Grice G.L., Nathan J.A.; RT "The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, RT control HIF1alpha prolyl hydroxylation by regulating cellular iron RT levels."; RL Elife 6:E22693-E22693(2017). RN [13] RP INTERACTION WITH SPAAR. RX PubMed=28024296; DOI=10.1038/nature21034; RA Matsumoto A., Pasut A., Matsumoto M., Yamashita R., Fung J., Monteleone E., RA Saghatelian A., Nakayama K.I., Clohessy J.G., Pandolfi P.P.; RT "mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR RT polypeptide."; RL Nature 541:228-232(2017). CC -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), CC a multisubunit enzyme composed of a peripheral complex (V1) that CC hydrolyzes ATP and a membrane integral complex (V0) that translocates CC protons (By similarity). V-ATPase is responsible for acidifying and CC maintaining the pH of intracellular compartments and in some cell CC types, is targeted to the plasma membrane, where it is responsible for CC acidifying the extracellular environment (By similarity). Essential CC component of the endosomal pH-sensing machinery (PubMed:16415858). May CC play a role in maintaining the Golgi functions, such as glycosylation CC maturation, by controlling the Golgi pH (PubMed:18157129). In aerobic CC conditions, involved in intracellular iron homeostasis, thus triggering CC the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to CC HIF1A hydroxylation and subsequent proteasomal degradation CC (PubMed:28296633). {ECO:0000250|UniProtKB:Q29466, CC ECO:0000250|UniProtKB:Q93050, ECO:0000269|PubMed:16415858, CC ECO:0000269|PubMed:18157129, ECO:0000269|PubMed:28296633}. CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two CC complexes: the ATP-hydrolytic V1 complex and the proton translocation CC V0 complex (By similarity). The V1 complex consists of three catalytic CC AB heterodimers that form a heterohexamer, three peripheral stalks each CC consisting of EG heterodimers, one central rotor including subunits D CC and F, and the regulatory subunits C and H (By similarity). The proton CC translocation complex V0 consists of the proton transport subunit a, a CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By CC similarity). Directly interacts with PSCD2 through its N-terminal CC cytosolic tail in an intra-endosomal acidification-dependent manner CC (PubMed:16415858). Disruption of this interaction results in the CC inhibition of endocytosis (PubMed:16415858). Interacts with SPAAR CC (PubMed:28024296). {ECO:0000250|UniProtKB:Q93050, CC ECO:0000269|PubMed:16415858, ECO:0000269|PubMed:28024296}. CC -!- INTERACTION: CC Q9Y487; Q99418: CYTH2; NbExp=2; IntAct=EBI-988630, EBI-448974; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Endosome membrane. Note=In kidney proximal tubules, also detected in CC subapical vesicles. {ECO:0000250}. CC -!- DISEASE: Cutis laxa, autosomal recessive, 2A (ARCL2A) [MIM:219200]: A CC disorder characterized by an excessive congenital skin wrinkling, a CC large fontanelle with delayed closure, a typical facial appearance with CC downslanting palpebral fissures, a general connective tissue weakness, CC and varying degrees of growth and developmental delay and neurological CC abnormalities. Some affected individuals develop seizures and mental CC deterioration later in life, whereas the skin phenotype tends to become CC milder with age. At the molecular level, an abnormal glycosylation of CC serum proteins is observed in many cases. CC {ECO:0000269|PubMed:18157129}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Wrinkly skin syndrome (WSS) [MIM:278250]: A rare autosomal CC recessive disorder characterized by wrinkling of the skin of the dorsum CC of the hands and feet, an increased number of palmar and plantar CC creases, wrinkled abdominal skin, multiple musculoskeletal CC abnormalities, microcephaly, growth failure and developmental delay. CC {ECO:0000269|PubMed:18157129}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family. CC {ECO:0000305}. CC -!- CAUTION: The N-terminal peptide may increase IL1B secretion by CC peripheral blood monocytes; however as this region is probably in the CC cytosol, the in vivo relevance of this observation needs to be CC confirmed. {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; AF112972; AAD04632.1; -; mRNA. DR EMBL; AK289391; BAF82080.1; -; mRNA. DR EMBL; CH471054; EAW98434.1; -; Genomic_DNA. DR EMBL; BC068531; AAH68531.1; -; mRNA. DR CCDS; CCDS9254.1; -. DR RefSeq; NP_036595.2; NM_012463.3. DR AlphaFoldDB; Q9Y487; -. DR SMR; Q9Y487; -. DR BioGRID; 117089; 161. DR ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant. DR IntAct; Q9Y487; 53. DR MINT; Q9Y487; -. DR STRING; 9606.ENSP00000332247; -. DR DrugBank; DB01133; Tiludronic acid. DR GlyConnect; 1898; 2 N-Linked glycans (1 site). DR GlyCosmos; Q9Y487; 2 sites, 2 glycans. DR GlyGen; Q9Y487; 3 sites, 2 N-linked glycans (1 site). DR iPTMnet; Q9Y487; -. DR PhosphoSitePlus; Q9Y487; -. DR SwissPalm; Q9Y487; -. DR BioMuta; ATP6V0A2; -. DR DMDM; 172046607; -. DR EPD; Q9Y487; -. DR jPOST; Q9Y487; -. DR MassIVE; Q9Y487; -. DR MaxQB; Q9Y487; -. DR PaxDb; 9606-ENSP00000332247; -. DR PeptideAtlas; Q9Y487; -. DR ProteomicsDB; 86130; -. DR Pumba; Q9Y487; -. DR Antibodypedia; 31833; 132 antibodies from 25 providers. DR DNASU; 23545; -. DR Ensembl; ENST00000330342.8; ENSP00000332247.2; ENSG00000185344.15. DR GeneID; 23545; -. DR KEGG; hsa:23545; -. DR MANE-Select; ENST00000330342.8; ENSP00000332247.2; NM_012463.4; NP_036595.2. DR UCSC; uc001ufr.4; human. DR AGR; HGNC:18481; -. DR CTD; 23545; -. DR DisGeNET; 23545; -. DR GeneCards; ATP6V0A2; -. DR GeneReviews; ATP6V0A2; -. DR HGNC; HGNC:18481; ATP6V0A2. DR HPA; ENSG00000185344; Low tissue specificity. DR MalaCards; ATP6V0A2; -. DR MIM; 219200; phenotype. DR MIM; 278250; phenotype. DR MIM; 611716; gene. DR neXtProt; NX_Q9Y487; -. DR OpenTargets; ENSG00000185344; -. DR Orphanet; 357074; Autosomal recessive cutis laxa type 2, classic type. DR Orphanet; 2834; Wrinkly skin syndrome. DR PharmGKB; PA38549; -. DR VEuPathDB; HostDB:ENSG00000185344; -. DR eggNOG; KOG2189; Eukaryota. DR GeneTree; ENSGT00950000182881; -. DR HOGENOM; CLU_005230_0_0_1; -. DR InParanoid; Q9Y487; -. DR OMA; TYVQLYI; -. DR OrthoDB; 1967517at2759; -. DR PhylomeDB; Q9Y487; -. DR TreeFam; TF300346; -. DR BioCyc; MetaCyc:G66-33375-MONOMER; -. DR BRENDA; 7.1.2.1; 2681. DR PathwayCommons; Q9Y487; -. DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes. DR Reactome; R-HSA-77387; Insulin receptor recycling. DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling. DR Reactome; R-HSA-983712; Ion channel transport. DR SignaLink; Q9Y487; -. DR BioGRID-ORCS; 23545; 34 hits in 1162 CRISPR screens. DR ChiTaRS; ATP6V0A2; human. DR GeneWiki; ATP6V0A2; -. DR GenomeRNAi; 23545; -. DR Pharos; Q9Y487; Tbio. DR PRO; PR:Q9Y487; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9Y487; Protein. DR Bgee; ENSG00000185344; Expressed in skin of leg and 156 other cell types or tissues. DR ExpressionAtlas; Q9Y487; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; NAS:ComplexPortal. DR GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl. DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central. DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB. DR GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; NAS:ComplexPortal. DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL. DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central. DR InterPro; IPR002490; V-ATPase_116kDa_su. DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka. DR PANTHER; PTHR11629:SF22; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 2; 1. DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1. DR Pfam; PF01496; V_ATPase_I; 1. DR PIRSF; PIRSF001293; ATP6V0A1; 1. DR Genevisible; Q9Y487; HS. PE 1: Evidence at protein level; KW Cell membrane; Endosome; Glycoprotein; Hydrogen ion transport; KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..856 FT /note="V-type proton ATPase 116 kDa subunit a 2" FT /id="PRO_0000119216" FT TOPO_DOM 1..393 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 394..412 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 413..414 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 415..431 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 432..445 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 446..475 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 476..549 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 550..569 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 570..587 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 588..608 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 609..651 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 652..671 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 672..739 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 740..764 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 765..785 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 786..824 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 825..856 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 700 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15920" FT CARBOHYD 484 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 505 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 685 FT /note="R -> Q (in dbSNP:rs7969410)" FT /id="VAR_042730" FT VARIANT 813 FT /note="A -> V (in dbSNP:rs17883456)" FT /id="VAR_042731" FT CONFLICT 428 FT /note="L -> W (in Ref. 1; AAD04632)" FT /evidence="ECO:0000305" FT CONFLICT 669 FT /note="L -> P (in Ref. 2; BAF82080)" FT /evidence="ECO:0000305" SQ SEQUENCE 856 AA; 98082 MW; 6C38B36FA33A92BA CRC64; MGSLFRSETM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK FVGEVKRCEE LERILVYLVQ EINRADIPLP EGEASPPAPP LKQVLEMQEQ LQKLEVELRE VTKNKEKLRK NLLELIEYTH MLRVTKTFVK RNVEFEPTYE EFPSLESDSL LDYSCMQRLG AKLGFVSGLI NQGKVEAFEK MLWRVCKGYT IVSYAELDES LEDPETGEVI KWYVFLISFW GEQIGHKVKK ICDCYHCHVY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVYSRVI QVKKMKAIYH MLNMCSFDVT NKCLIAEVWC PEADLQDLRR ALEEGSRESG ATIPSFMNII PTKETPPTRI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT IITFPFLFAV MFGDFGHGFV MFLFALLLVL NENHPRLNQS QEIMRMFFNG RYILLLMGLF SVYTGLIYND CFSKSVNLFG SGWNVSAMYS SSHPPAEHKK MVLWNDSVVR HNSILQLDPS IPGVFRGPYP LGIDPIWNLA TNRLTFLNSF KMKMSVILGI IHMTFGVILG IFNHLHFRKK FNIYLVSIPE LLFMLCIFGY LIFMIFYKWL VFSAETSRVA PSILIEFINM FLFPASKTSG LYTGQEYVQR VLLVVTALSV PVLFLGKPLF LLWLHNGRSC FGVNRSGYTL IRKDSEEEVS LLGSQDIEEG NHQVEDGCRE MACEEFNFGE ILMTQVIHSI EYCLGCISNT ASYLRLWALS LAHAQLSDVL WAMLMRVGLR VDTTYGVLLL LPVIALFAVL TIFILLIMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF SFSLLSSKFN NDDSVA //