ID   VATO_HUMAN              Reviewed;         205 AA.
AC   Q99437; D3DPY5; Q6IB32;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   18-JUN-2025, entry version 199.
DE   RecName: Full=V-type proton ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE            Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE   AltName: Full=Vacuolar proton pump 21 kDa proteolipid subunit c'' {ECO:0000305};
DE   AltName: Full=hATPL;
GN   Name=ATP6V0B; Synonyms=ATP6F;
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).
RC   TISSUE=Kidney;
RX   PubMed=9653649; DOI=10.1006/geno.1998.5310;
RA   Nishigori H., Yamada S., Tomura H., Fernald A.A., le Beau M.M.,
RA   Takeuchi T., Takeda J.;
RT   "Identification and characterization of the gene encoding a second
RT   proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F).";
RL   Genomics 50:222-228(1998).
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] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [7] {ECO:0007744|PDB:6WLW, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, AND
RP   IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX   PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA   Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT   "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT   Assembly.";
RL   Mol. Cell 80:501-511.e3(2020).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] MET-155.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Proton-conducting pore forming subunit of the V0 complex of
CC       vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC       peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC       complex (V0) that translocates protons (PubMed:33065002). V-ATPase is
CC       responsible for acidifying and maintaining the pH of intracellular
CC       compartments and in some cell types, is targeted to the plasma
CC       membrane, where it is responsible for acidifying the extracellular
CC       environment (By similarity). {ECO:0000250|UniProtKB:Q2TA24,
CC       ECO:0000269|PubMed:33065002}.
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 (PubMed:33065002). The V1 complex consists of three
CC       catalytic AB heterodimers that form a heterohexamer, three peripheral
CC       stalks each consisting of EG heterodimers, one central rotor including
CC       subunits D and F, and the regulatory subunits C and H
CC       (PubMed:33065002). The proton translocation complex V0 consists of the
CC       proton transport subunit a, a ring of proteolipid subunits c9c'',
CC       rotary subunit d, subunits e and f, and the accessory subunits
CC       ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with IFITM3
CC       (By similarity). Interacts with TM4SF19; this interaction inhibits V1-
CC       V0 complex assembly (By similarity). {ECO:0000250|UniProtKB:Q91V37,
CC       ECO:0000269|PubMed:33065002}.
CC   -!- INTERACTION:
CC       Q99437; Q86Y34: ADGRG3; NbExp=3; IntAct=EBI-3904417, EBI-17979264;
CC       Q99437; P05090: APOD; NbExp=3; IntAct=EBI-3904417, EBI-715495;
CC       Q99437; P29400-2: COL4A5; NbExp=3; IntAct=EBI-3904417, EBI-12211159;
CC       Q99437; P54849: EMP1; NbExp=3; IntAct=EBI-3904417, EBI-4319440;
CC       Q99437; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-3904417, EBI-18938272;
CC       Q99437; P48165: GJA8; NbExp=3; IntAct=EBI-3904417, EBI-17458373;
CC       Q99437; O15529: GPR42; NbExp=3; IntAct=EBI-3904417, EBI-18076404;
CC       Q99437; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-3904417, EBI-12808020;
CC       Q99437; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-3904417, EBI-8503746;
CC       Q99437; P26715: KLRC1; NbExp=3; IntAct=EBI-3904417, EBI-9018187;
CC       Q99437; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3904417, EBI-11956541;
CC       Q99437; P30301: MIP; NbExp=3; IntAct=EBI-3904417, EBI-8449636;
CC       Q99437; Q96HJ5: MS4A3; NbExp=5; IntAct=EBI-3904417, EBI-12806656;
CC       Q99437; Q8IXM6: NRM; NbExp=3; IntAct=EBI-3904417, EBI-10262547;
CC       Q99437; Q14973: SLC10A1; NbExp=3; IntAct=EBI-3904417, EBI-3923031;
CC       Q99437; P22732: SLC2A5; NbExp=3; IntAct=EBI-3904417, EBI-2825135;
CC       Q99437; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-3904417, EBI-17498703;
CC       Q99437; P27105: STOM; NbExp=3; IntAct=EBI-3904417, EBI-1211440;
CC       Q99437; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-3904417, EBI-6448756;
CC       Q99437; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-3904417, EBI-10315004;
CC       Q99437; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-3904417, EBI-1055364;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:Q2TA24}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99437-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99437-2; Sequence=VSP_046288;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; D89052; BAA13753.1; -; mRNA.
DR   EMBL; BT007151; AAP35815.1; -; mRNA.
DR   EMBL; CR456972; CAG33253.1; -; mRNA.
DR   EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07066.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07067.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07068.1; -; Genomic_DNA.
DR   EMBL; BC000423; AAH00423.1; -; mRNA.
DR   EMBL; BC005876; AAH05876.1; -; mRNA.
DR   CCDS; CCDS41315.1; -. [Q99437-2]
DR   CCDS; CCDS505.1; -. [Q99437-1]
DR   RefSeq; NP_001034546.1; NM_001039457.3. [Q99437-2]
DR   RefSeq; NP_004038.1; NM_004047.5. [Q99437-1]
DR   RefSeq; XP_047278606.1; XM_047422650.1. [Q99437-2]
DR   RefSeq; XP_054193068.1; XM_054337093.1. [Q99437-2]
DR   PDB; 6WLW; EM; 3.00 A; 0=1-205.
DR   PDB; 6WM2; EM; 3.10 A; 0=1-205.
DR   PDB; 6WM3; EM; 3.40 A; 0=1-205.
DR   PDB; 6WM4; EM; 3.60 A; 0=1-205.
DR   PDB; 7U4T; EM; 3.60 A; 0=1-205.
DR   PDB; 7UNF; EM; 4.08 A; 1=1-205.
DR   PDBsum; 6WLW; -.
DR   PDBsum; 6WM2; -.
DR   PDBsum; 6WM3; -.
DR   PDBsum; 6WM4; -.
DR   PDBsum; 7U4T; -.
DR   PDBsum; 7UNF; -.
DR   AlphaFoldDB; Q99437; -.
DR   EMDB; EMD-21844; -.
DR   EMDB; EMD-21847; -.
DR   EMDB; EMD-21848; -.
DR   EMDB; EMD-21849; -.
DR   EMDB; EMD-26334; -.
DR   EMDB; EMD-26623; -.
DR   SMR; Q99437; -.
DR   BioGRID; 107016; 38.
DR   ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant.
DR   ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant.
DR   ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant.
DR   ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant.
DR   FunCoup; Q99437; 1295.
DR   IntAct; Q99437; 26.
DR   MINT; Q99437; -.
DR   STRING; 9606.ENSP00000434729; -.
DR   DrugBank; DB01133; Tiludronic acid.
DR   iPTMnet; Q99437; -.
DR   PhosphoSitePlus; Q99437; -.
DR   BioMuta; ATP6V0B; -.
DR   DMDM; 6136172; -.
DR   MassIVE; Q99437; -.
DR   PaxDb; 9606-ENSP00000434729; -.
DR   PeptideAtlas; Q99437; -.
DR   Antibodypedia; 32422; 87 antibodies from 18 providers.
DR   DNASU; 533; -.
DR   Ensembl; ENST00000236067.8; ENSP00000236067.4; ENSG00000117410.14. [Q99437-2]
DR   Ensembl; ENST00000472174.7; ENSP00000431605.1; ENSG00000117410.14. [Q99437-1]
DR   Ensembl; ENST00000498664.1; ENSP00000434094.1; ENSG00000117410.14. [Q99437-2]
DR   GeneID; 533; -.
DR   KEGG; hsa:533; -.
DR   MANE-Select; ENST00000472174.7; ENSP00000431605.1; NM_004047.5; NP_004038.1.
DR   UCSC; uc001cld.4; human. [Q99437-1]
DR   AGR; HGNC:861; -.
DR   CTD; 533; -.
DR   DisGeNET; 533; -.
DR   GeneCards; ATP6V0B; -.
DR   HGNC; HGNC:861; ATP6V0B.
DR   HPA; ENSG00000117410; Low tissue specificity.
DR   MIM; 603717; gene.
DR   OpenTargets; ENSG00000117410; -.
DR   VEuPathDB; HostDB:ENSG00000117410; -.
DR   eggNOG; KOG0233; Eukaryota.
DR   GeneTree; ENSGT00550000075120; -.
DR   HOGENOM; CLU_085752_0_0_1; -.
DR   InParanoid; Q99437; -.
DR   OMA; TSPYMWG; -.
DR   OrthoDB; 10264021at2759; -.
DR   PAN-GO; Q99437; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q99437; -.
DR   BioCyc; MetaCyc:ENSG00000117410-MONOMER; -.
DR   PathwayCommons; Q99437; -.
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-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-HSA-983712; Ion channel transport.
DR   Reactome; R-HSA-9857377; Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy.
DR   SignaLink; Q99437; -.
DR   SIGNOR; Q99437; -.
DR   BioGRID-ORCS; 533; 711 hits in 1169 CRISPR screens.
DR   ChiTaRS; ATP6V0B; human.
DR   GeneWiki; ATP6V0B; -.
DR   GenomeRNAi; 533; -.
DR   Pharos; Q99437; Tbio.
DR   PRO; PR:Q99437; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q99437; protein.
DR   Bgee; ENSG00000117410; Expressed in granulocyte and 202 other cell types or tissues.
DR   ExpressionAtlas; Q99437; baseline and differential.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; NAS:ComplexPortal.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0051452; P:intracellular pH reduction; NAS:ComplexPortal.
DR   GO; GO:0007042; P:lysosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc.
DR   GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0007035; P:vacuolar acidification; NAS:ComplexPortal.
DR   CDD; cd18177; ATP-synt_Vo_c_ATP6F_rpt1; 1.
DR   CDD; cd18178; ATP-synt_Vo_c_ATP6F_rpt2; 1.
DR   FunFam; 1.20.120.610:FF:000002; V-type proton ATPase proteolipid subunit; 1.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
DR   neXtProt; NX_Q99437; -.
DR   PharmGKB; PA25148; -.
DR   TreeFam; TF314946; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW   Hydrogen ion transport; Ion transport; Membrane; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..205
FT                   /note="V-type proton ATPase 21 kDa proteolipid subunit c''"
FT                   /id="PRO_0000071777"
FT   TOPO_DOM        1..3
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..90
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..175
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   SITE            98
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TA24"
FT   VAR_SEQ         1..47
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046288"
FT   VARIANT         155
FT                   /note="V -> M (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs373883976)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035703"
FT   HELIX           3..28
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           46..79
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           91..111
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           123..168
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:6WLW"
FT   HELIX           173..197
FT                   /evidence="ECO:0007829|PDB:6WLW"
SQ   SEQUENCE   205 AA;  21406 MW;  F17C688D068A2785 CRC64;
     MTGLALLYSG VFVAFWACAL AVGVCYTIFD LGFRFDVAWF LTETSPFMWS NLGIGLAISL
     SVVGAAWGIY ITGSSIIGGG VKAPRIKTKN LVSIIFCEAV AIYGIIMAIV ISNMAEPFSA
     TDPKAIGHRN YHAGYSMFGA GLTVGLSNLF CGVCVGIVGS GAALADAQNP SLFVKILIVE
     IFGSAIGLFG VIVAILQTSR VKMGD
//