VPP2_HUMAN
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 03-AUG-2022, entry version 184.
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; 148.
DR ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant.
DR IntAct; Q9Y487; 51.
DR MINT; Q9Y487; -.
DR STRING; 9606.ENSP00000332247; -.
DR DrugBank; DB01133; Tiludronic acid.
DR GlyConnect; 1898; 2 N-Linked glycans (1 site).
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; Q9Y487; -.
DR PeptideAtlas; Q9Y487; -.
DR PRIDE; Q9Y487; -.
DR ProteomicsDB; 86130; -.
DR Antibodypedia; 31833; 115 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 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; MIFFKWL; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q9Y487; -.
DR TreeFam; TF300346; -.
DR BioCyc; MetaCyc:G66-33375-MON; -.
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; 26 hits in 1075 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 155 other tissues.
DR ExpressionAtlas; Q9Y487; baseline and differential.
DR Genevisible; Q9Y487; HS.
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; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IC:ComplexPortal.
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:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:1902600; P:proton transmembrane transport; IC: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; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
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
