VPP3_HUMAN
ID VPP3_HUMAN Reviewed; 830 AA.
AC Q13488; O75877; Q8WVC5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 3;
DE Short=V-ATPase 116 kDa subunit a 3;
DE AltName: Full=Osteoclastic proton pump 116 kDa subunit;
DE Short=OC-116 kDa;
DE Short=OC116;
DE AltName: Full=T-cell immune regulator 1;
DE AltName: Full=T-cell immune response cDNA7 protein;
DE Short=TIRC7;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3;
GN Name=TCIRG1; Synonyms=ATP6N1C, ATP6V0A3;
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 LONG).
RC TISSUE=Osteoclastoma;
RX PubMed=8579597; DOI=10.1006/bbrc.1996.0145;
RA Li Y.P., Chen W., Stashenko P.;
RT "Molecular cloning and characterization of a putative novel human
RT osteoclast-specific 116-kDa vacuolar proton pump subunit.";
RL Biochem. Biophys. Res. Commun. 218:813-821(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA Utku N., Heinemann T., Bulwin C.-G., Beinke S., Beato F., Randall J.,
RA Busconi L., Delphire E., Robertson E.R., Kojima R., Volk H.D.,
RA Milford E.L., Gullans S.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), AND FUNCTION.
RX PubMed=10329006; DOI=10.1006/geno.1999.5751;
RA Heinemann T., Bulwin G.C., Randall J., Schnieders B., Sandhoff K.,
RA Volk H.D., Milford E., Gullans S.R., Utku N.;
RT "Genomic organization of the gene coding for TIRC7, a novel membrane
RT protein essential for T cell activation.";
RL Genomics 57:398-406(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Lung, and Pancreas;
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 VARIANTS OPTB1 ARG-405 AND LEU-444.
RX PubMed=11532986; DOI=10.1093/hmg/10.17.1767;
RA Sobacchi C., Frattini A., Orchard P., Porras O., Tezcan I., Andolina M.,
RA Babul-Hirji R., Baric I., Canham N., Chitayat D., Dupuis-Girod S.,
RA Ellis I., Etzioni A., Fasth A., Fisher A., Gerritsen B., Gulino V.,
RA Horwitz E., Klamroth V., Lanino E., Mirolo M., Musio A., Matthijs G.,
RA Nonomaya S., Notarangelo L.D., Ochs H.D., Superti-Furga A., Valiaho J.,
RA van Hove J.L.K., Vihinen M., Vujic D., Vezzoni P., Villa A.;
RT "The mutational spectrum of human malignant autosomal recessive
RT osteopetrosis.";
RL Hum. Mol. Genet. 10:1767-1773(2001).
RN [7]
RP VARIANT OPTB1 ARG-405.
RX PubMed=12552563; DOI=10.1002/humu.10165;
RA Scimeca J.-C., Quincey D., Parrinello H., Romatet D., Grosgeorge J.,
RA Gaudray P., Philip N., Fischer A., Carle G.F.;
RT "Novel mutations in the TCIRG1 gene encoding the a3 subunit of the vacuolar
RT proton pump in patients affected by infantile malignant osteopetrosis.";
RL Hum. Mutat. 21:151-157(2003).
RN [8]
RP VARIANTS OPTB1 PRO-141; ARG-405; ASN-462 DEL; ASN-517 AND ARG-775.
RX PubMed=15300850; DOI=10.1002/humu.20076;
RA Susani L., Pangrazio A., Sobacchi C., Taranta A., Mortier G.,
RA Savarirayan R., Villa A., Orchard P., Vezzoni P., Albertini A.,
RA Frattini A., Pagani F.;
RT "TCIRG1-dependent recessive osteopetrosis: mutation analysis, functional
RT identification of the splicing defects, and in vitro rescue by U1 snRNA.";
RL Hum. Mutat. 24:225-235(2004).
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). Seems to be
CC directly involved in T-cell activation (PubMed:10329006).
CC {ECO:0000250|UniProtKB:Q29466, ECO:0000250|UniProtKB:Q93050,
CC ECO:0000269|PubMed:10329006}.
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). {ECO:0000250|UniProtKB:Q93050}.
CC -!- INTERACTION:
CC Q13488; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-3914669, EBI-1389308;
CC Q13488; O43711: TLX3; NbExp=3; IntAct=EBI-3914669, EBI-3939165;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q13488-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13488-2; Sequence=VSP_000345;
CC -!- TISSUE SPECIFICITY: Isoform long is highly expressed in osteoclastomas.
CC Isoform short is highly expressed in thymus.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 1 (OPTB1) [MIM:259700]: A
CC rare genetic disease characterized by abnormally dense bone, due to
CC defective resorption of immature bone. Osteopetrosis occurs in two
CC forms: a severe autosomal recessive form occurring in utero, infancy,
CC or childhood, and a benign autosomal dominant form occurring in
CC adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC early infancy with macrocephaly, feeding difficulties, evolving
CC blindness and deafness, bone marrow failure, severe anemia, and
CC hepatosplenomegaly. Deafness and blindness are generally thought to
CC represent effects of pressure on nerves. {ECO:0000269|PubMed:11532986,
CC ECO:0000269|PubMed:12552563, ECO:0000269|PubMed:15300850}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=TCIRG1base; Note=TCIRG1 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/TCIRG1base/";
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DR EMBL; U45285; AAA97878.1; -; mRNA.
DR EMBL; AF025374; AAC35742.1; -; mRNA.
DR EMBL; AF033033; AAD31081.2; -; Genomic_DNA.
DR EMBL; CH471076; EAW74691.1; -; Genomic_DNA.
DR EMBL; BC018133; AAH18133.1; -; mRNA.
DR EMBL; BC032465; AAH32465.1; -; mRNA.
DR CCDS; CCDS53670.1; -. [Q13488-2]
DR CCDS; CCDS8177.1; -. [Q13488-1]
DR RefSeq; NP_006010.2; NM_006019.3. [Q13488-1]
DR RefSeq; NP_006044.1; NM_006053.3. [Q13488-2]
DR RefSeq; XP_005273766.1; XM_005273709.3.
DR RefSeq; XP_011543028.1; XM_011544726.2.
DR AlphaFoldDB; Q13488; -.
DR SMR; Q13488; -.
DR BioGRID; 115597; 82.
DR ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant.
DR IntAct; Q13488; 16.
DR MINT; Q13488; -.
DR STRING; 9606.ENSP00000265686; -.
DR DrugBank; DB01133; Tiludronic acid.
DR DrugCentral; Q13488; -.
DR iPTMnet; Q13488; -.
DR PhosphoSitePlus; Q13488; -.
DR BioMuta; TCIRG1; -.
DR DMDM; 223634720; -.
DR EPD; Q13488; -.
DR jPOST; Q13488; -.
DR MassIVE; Q13488; -.
DR MaxQB; Q13488; -.
DR PaxDb; Q13488; -.
DR PeptideAtlas; Q13488; -.
DR PRIDE; Q13488; -.
DR ProteomicsDB; 59481; -. [Q13488-1]
DR ProteomicsDB; 59482; -. [Q13488-2]
DR Antibodypedia; 30523; 98 antibodies from 28 providers.
DR DNASU; 10312; -.
DR Ensembl; ENST00000265686.8; ENSP00000265686.3; ENSG00000110719.10. [Q13488-1]
DR Ensembl; ENST00000532635.5; ENSP00000434407.1; ENSG00000110719.10. [Q13488-2]
DR GeneID; 10312; -.
DR KEGG; hsa:10312; -.
DR MANE-Select; ENST00000265686.8; ENSP00000265686.3; NM_006019.4; NP_006010.2.
DR UCSC; uc001one.4; human. [Q13488-1]
DR CTD; 10312; -.
DR DisGeNET; 10312; -.
DR GeneCards; TCIRG1; -.
DR HGNC; HGNC:11647; TCIRG1.
DR HPA; ENSG00000110719; Tissue enhanced (pancreas).
DR MalaCards; TCIRG1; -.
DR MIM; 259700; phenotype.
DR MIM; 604592; gene.
DR neXtProt; NX_Q13488; -.
DR OpenTargets; ENSG00000110719; -.
DR Orphanet; 486; Autosomal dominant severe congenital neutropenia.
DR Orphanet; 667; Autosomal recessive malignant osteopetrosis.
DR Orphanet; 1782; Dysosteosclerosis.
DR Orphanet; 210110; Intermediate osteopetrosis.
DR PharmGKB; PA36399; -.
DR VEuPathDB; HostDB:ENSG00000110719; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; Q13488; -.
DR OMA; SKIVKIC; -.
DR OrthoDB; 24858at2759; -.
DR PhylomeDB; Q13488; -.
DR TreeFam; TF300346; -.
DR BioCyc; MetaCyc:ENSG00000110719-MON; -.
DR PathwayCommons; Q13488; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
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 SignaLink; Q13488; -.
DR BioGRID-ORCS; 10312; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; TCIRG1; human.
DR GeneWiki; TCIRG1; -.
DR GenomeRNAi; 10312; -.
DR Pharos; Q13488; Tbio.
DR PRO; PR:Q13488; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13488; protein.
DR Bgee; ENSG00000110719; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; Q13488; baseline and differential.
DR Genevisible; Q13488; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR GO; GO:0097188; P:dentin mineralization; IEA:Ensembl.
DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0051650; P:establishment of vesicle localization; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0007042; P:lysosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; ISS:ParkinsonsUK-UCL.
DR GO; GO:0035709; P:memory T cell activation; IEA:Ensembl.
DR GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0090383; P:phagosome acidification; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; ISS:ParkinsonsUK-UCL.
DR GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0010155; P:regulation of proton transport; IEA:Ensembl.
DR GO; GO:0010272; P:response to silver ion; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0035711; P:T-helper 1 cell activation; IEA:Ensembl.
DR GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
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 Alternative splicing; Disease variant; Hydrogen ion transport;
KW Ion transport; Membrane; Osteopetrosis; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..830
FT /note="V-type proton ATPase 116 kDa subunit a 3"
FT /id="PRO_0000119218"
FT TOPO_DOM 1..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..406
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..532
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..635
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..766
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_000345"
FT VARIANT 56
FT /note="R -> W (in dbSNP:rs36027301)"
FT /id="VAR_054340"
FT VARIANT 141
FT /note="A -> P (in OPTB1)"
FT /evidence="ECO:0000269|PubMed:15300850"
FT /id="VAR_020988"
FT VARIANT 161
FT /note="P -> L (in dbSNP:rs34227834)"
FT /id="VAR_054341"
FT VARIANT 405
FT /note="G -> R (in OPTB1; dbSNP:rs137853150)"
FT /evidence="ECO:0000269|PubMed:11532986,
FT ECO:0000269|PubMed:12552563, ECO:0000269|PubMed:15300850"
FT /id="VAR_019569"
FT VARIANT 444
FT /note="R -> L (in OPTB1; dbSNP:rs137853151)"
FT /evidence="ECO:0000269|PubMed:11532986"
FT /id="VAR_019570"
FT VARIANT 462
FT /note="Missing (in OPTB1; dbSNP:rs771271907)"
FT /evidence="ECO:0000269|PubMed:15300850"
FT /id="VAR_020989"
FT VARIANT 517
FT /note="D -> N (in OPTB1; dbSNP:rs369264588)"
FT /evidence="ECO:0000269|PubMed:15300850"
FT /id="VAR_020990"
FT VARIANT 775
FT /note="P -> R (in OPTB1)"
FT /evidence="ECO:0000269|PubMed:15300850"
FT /id="VAR_020991"
FT CONFLICT 377
FT /note="A -> R (in Ref. 1; AAA97878)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="Missing (in Ref. 1; AAA97878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 92968 MW; 50751B41B171D9D2 CRC64;
MGSMFRSEEV ALVQLFLPTA AAYTCVSRLG ELGLVEFRDL NASVSAFQRR FVVDVRRCEE
LEKTFTFLQE EVRRAGLVLP PPKGRLPAPP PRDLLRIQEE TERLAQELRD VRGNQQALRA
QLHQLQLHAA VLRQGHEPQL AAAHTDGASE RTPLLQAPGG PHQDLRVNFV AGAVEPHKAP
ALERLLWRAC RGFLIASFRE LEQPLEHPVT GEPATWMTFL ISYWGEQIGQ KIRKITDCFH
CHVFPFLQQE EARLGALQQL QQQSQELQEV LGETERFLSQ VLGRVLQLLP PGQVQVHKMK
AVYLALNQCS VSTTHKCLIA EAWCSVRDLP ALQEALRDSS MEEGVSAVAH RIPCRDMPPT
LIRTNRFTAS FQGIVDAYGV GRYQEVNPAP YTIITFPFLF AVMFGDVGHG LLMFLFALAM
VLAENRPAVK AAQNEIWQTF FRGRYLLLLM GLFSIYTGFI YNECFSRATS IFPSGWSVAA
MANQSGWSDA FLAQHTMLTL DPNVTGVFLG PYPFGIDPIW SLAANHLSFL NSFKMKMSVI
LGVVHMAFGV VLGVFNHVHF GQRHRLLLET LPELTFLLGL FGYLVFLVIY KWLCVWAARA
ASAPSILIHF INMFLFSHSP SNRLLYPRQE VVQATLVVLA LAMVPILLLG TPLHLLHRHR
RRLRRRPADR QEENKAGLLD LPDASVNGWS SDEEKAGGLD DEEEAELVPS EVLMHQAIHT
IEFCLGCVSN TASYLRLWAL SLAHAQLSEV LWAMVMRIGL GLGREVGVAA VVLVPIFAAF
AVMTVAILLV MEGLSAFLHA LRLHWVEFQN KFYSGTGYKL SPFTFAATDD
