ID   P2RX5_HUMAN             Reviewed;         422 AA.
AC   Q93086; G5E981; O43450; O75540; Q308M5; Q59F38; Q8IXW4; Q93087; Q9NZV0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 4.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=P2X purinoceptor 5;
DE            Short=P2X5;
DE   AltName: Full=ATP receptor;
DE   AltName: Full=Purinergic receptor;
GN   Name=P2RX5; Synonyms=P2X5;
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] (ISOFORMS 2 AND 3).
RA   Tokuyama Y., Mereu L., Chen X., Rouard M., Bell G.I.;
RT   "Cloning of human P2X purinoceptor new subtype (P2X5).";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9414125; DOI=10.1016/s0014-5793(97)01380-x;
RA   Le K.-T., Paquet M., Nouel D., Babinski K., Seguela P.;
RT   "Primary structure and expression of a naturally truncated human P2X ATP
RT   receptor subunit from brain and immune system.";
RL   FEBS Lett. 418:195-199(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10673275; DOI=10.1101/gr.10.2.165;
RA   Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G.,
RA   Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
RA   Green E.D.;
RT   "The genomic region encompassing the nephropathic cystinosis gene (CTNS):
RT   complete sequencing of a 200-kb segment and discovery of a novel gene
RT   within the common cystinosis-causing deletion.";
RL   Genome Res. 10:165-173(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA   Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA   Tang Z., Huang B., Lin L., Yang S.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Erythroleukemia, and Mesangial cell;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [9]
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Leukocyte, and Lung;
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).
CC   -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC   -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC       trimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q93086-3; Sequence=Displayed;
CC       Name=2; Synonyms=A;
CC         IsoId=Q93086-1; Sequence=VSP_035587;
CC       Name=3; Synonyms=B;
CC         IsoId=Q93086-2; Sequence=VSP_004503, VSP_035587;
CC       Name=4;
CC         IsoId=Q93086-4; Sequence=VSP_035588;
CC       Name=5;
CC         IsoId=Q93086-5; Sequence=VSP_004503;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in brain and immune
CC       system.
CC   -!- MISCELLANEOUS: [Isoform 4]: 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 P2X receptor family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF43106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AK307959; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD92860.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BC028084; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=P2X receptor entry;
CC       URL="https://en.wikipedia.org/wiki/P2X_receptor";
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DR   EMBL; U49395; AAB08576.1; -; mRNA.
DR   EMBL; U49396; AAB08577.1; -; mRNA.
DR   EMBL; AF016709; AAC51931.1; -; mRNA.
DR   EMBL; AF168787; AAF43105.1; -; Genomic_DNA.
DR   EMBL; AF168787; AAF43106.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF070573; AAC28645.1; -; mRNA.
DR   EMBL; DQ234349; ABB29978.1; -; mRNA.
DR   EMBL; AK290889; BAF83578.1; -; mRNA.
DR   EMBL; AK307959; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB209623; BAD92860.1; ALT_FRAME; mRNA.
DR   EMBL; AC132942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90483.1; -; Genomic_DNA.
DR   EMBL; BC028084; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC039015; AAH39015.1; -; mRNA.
DR   CCDS; CCDS11034.1; -. [Q93086-3]
DR   CCDS; CCDS11035.1; -. [Q93086-2]
DR   CCDS; CCDS56014.1; -. [Q93086-5]
DR   CCDS; CCDS56015.1; -. [Q93086-1]
DR   RefSeq; NP_001191448.1; NM_001204519.1. [Q93086-1]
DR   RefSeq; NP_001191449.1; NM_001204520.1. [Q93086-5]
DR   RefSeq; NP_002552.2; NM_002561.3. [Q93086-3]
DR   RefSeq; NP_778255.1; NM_175080.2. [Q93086-2]
DR   AlphaFoldDB; Q93086; -.
DR   SMR; Q93086; -.
DR   BioGRID; 111065; 71.
DR   IntAct; Q93086; 25.
DR   STRING; 9606.ENSP00000225328; -.
DR   BindingDB; Q93086; -.
DR   ChEMBL; CHEMBL4942; -.
DR   DrugBank; DB01069; Promethazine.
DR   TCDB; 1.A.7.1.11; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR   GlyCosmos; Q93086; 2 sites, No reported glycans.
DR   GlyGen; Q93086; 3 sites.
DR   iPTMnet; Q93086; -.
DR   PhosphoSitePlus; Q93086; -.
DR   BioMuta; P2RX5; -.
DR   DMDM; 209572778; -.
DR   jPOST; Q93086; -.
DR   MassIVE; Q93086; -.
DR   MaxQB; Q93086; -.
DR   PaxDb; 9606-ENSP00000225328; -.
DR   PeptideAtlas; Q93086; -.
DR   ProteomicsDB; 33860; -.
DR   ProteomicsDB; 75715; -. [Q93086-3]
DR   ProteomicsDB; 75716; -. [Q93086-1]
DR   ProteomicsDB; 75717; -. [Q93086-2]
DR   ProteomicsDB; 75718; -. [Q93086-4]
DR   Antibodypedia; 10941; 245 antibodies from 27 providers.
DR   DNASU; 5026; -.
DR   Ensembl; ENST00000225328.10; ENSP00000225328.5; ENSG00000083454.23. [Q93086-3]
DR   Ensembl; ENST00000345901.7; ENSP00000342161.3; ENSG00000083454.23. [Q93086-5]
DR   Ensembl; ENST00000547178.5; ENSP00000448355.1; ENSG00000083454.23. [Q93086-1]
DR   Ensembl; ENST00000551178.5; ENSP00000447545.1; ENSG00000083454.23. [Q93086-2]
DR   GeneID; 5026; -.
DR   KEGG; hsa:5026; -.
DR   MANE-Select; ENST00000225328.10; ENSP00000225328.5; NM_002561.4; NP_002552.2.
DR   UCSC; uc002fwi.4; human. [Q93086-3]
DR   AGR; HGNC:8536; -.
DR   CTD; 5026; -.
DR   DisGeNET; 5026; -.
DR   GeneCards; P2RX5; -.
DR   HGNC; HGNC:8536; P2RX5.
DR   HPA; ENSG00000083454; Tissue enhanced (intestine, lymphoid tissue).
DR   MIM; 602836; gene.
DR   neXtProt; NX_Q93086; -.
DR   OpenTargets; ENSG00000083454; -.
DR   PharmGKB; PA32865; -.
DR   VEuPathDB; HostDB:ENSG00000083454; -.
DR   eggNOG; ENOG502QSUI; Eukaryota.
DR   GeneTree; ENSGT01020000230351; -.
DR   InParanoid; Q93086; -.
DR   OMA; GIHIEWN; -.
DR   OrthoDB; 5312692at2759; -.
DR   PhylomeDB; Q93086; -.
DR   TreeFam; TF328633; -.
DR   PathwayCommons; Q93086; -.
DR   Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-HSA-418346; Platelet homeostasis.
DR   SignaLink; Q93086; -.
DR   BioGRID-ORCS; 5026; 18 hits in 1148 CRISPR screens.
DR   GeneWiki; P2RX5; -.
DR   GenomeRNAi; 5026; -.
DR   Pharos; Q93086; Tchem.
DR   PRO; PR:Q93086; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q93086; Protein.
DR   Bgee; ENSG00000083454; Expressed in spleen and 143 other cell types or tissues.
DR   ExpressionAtlas; Q93086; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; NAS:BHF-UCL.
DR   GO; GO:0004931; F:extracellularly ATP-gated monoatomic cation channel activity; IBA:GO_Central.
DR   GO; GO:0005216; F:monoatomic ion channel activity; TAS:ProtInc.
DR   GO; GO:0001614; F:purinergic nucleotide receptor activity; NAS:BHF-UCL.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; NAS:BHF-UCL.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; NAS:BHF-UCL.
DR   GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.10.287.940; atp-gated p2x4 ion channel; 1.
DR   Gene3D; 2.60.490.10; atp-gated p2x4 ion channel domain; 1.
DR   InterPro; IPR003048; P2X5_purnocptor.
DR   InterPro; IPR027309; P2X_extracellular_dom_sf.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   NCBIfam; TIGR00863; P2X; 1.
DR   PANTHER; PTHR10125; P2X PURINOCEPTOR; 1.
DR   PANTHER; PTHR10125:SF12; P2X PURINOCEPTOR 5; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01312; P2X5RECEPTOR.
DR   PRINTS; PR01307; P2XRECEPTOR.
DR   PROSITE; PS01212; P2X_RECEPTOR; 1.
DR   Genevisible; Q93086; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..422
FT                   /note="P2X purinoceptor 5"
FT                   /id="PRO_0000161555"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..319
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          356..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..169
FT                   /evidence="ECO:0000250"
FT   DISULFID        129..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        135..163
FT                   /evidence="ECO:0000250"
FT   DISULFID        220..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..272
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         97..120
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.4,
FT                   ECO:0000303|Ref.5"
FT                   /id="VSP_004503"
FT   VAR_SEQ         205..206
FT                   /note="KS -> N (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9414125, ECO:0000303|Ref.1,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_035587"
FT   VAR_SEQ         421..422
FT                   /note="ST -> LRTPSASPLHQE (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.7"
FT                   /id="VSP_035588"
FT   CONFLICT        96
FT                   /note="Q -> E (in Ref. 1; AAB08577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97..98
FT                   /note="GE -> EK (in Ref. 1; AAB08576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="E -> G (in Ref. 2; AAC51931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..238
FT                   /note="VI -> IV (in Ref. 2; AAC51931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="E -> R (in Ref. 2; AAC51931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="F -> S (in Ref. 1; AAB08576/AAB08577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="K -> R (in Ref. 5; ABB29978)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="E -> Q (in Ref. 1; AAB08576/AAB08577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399..400
FT                   /note="KR -> NV (in Ref. 1; AAB08576/AAB08577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  47205 MW;  B122027A23B2A240 CRC64;
     MGQAGCKGLC LSLFDYKTEK YVIAKNKKVG LLYRLLQASI LAYLVVWVFL IKKGYQDVDT
     SLQSAVITKV KGVAFTNTSD LGQRIWDVAD YVIPAQGENV FFVVTNLIVT PNQRQNVCAE
     NEGIPDGACS KDSDCHAGEA VTAGNGVKTG RCLRRENLAR GTCEIFAWCP LETSSRPEEP
     FLKEAEDFTI FIKNHIRFPK FNFSKSNVMD VKDRSFLKSC HFGPKNHYCP IFRLGSVIRW
     AGSDFQDIAL EGGVIGINIE WNCDLDKAAS ECHPHYSFSR LDNKLSKSVS SGYNFRFARY
     YRDAAGVEFR TLMKAYGIRF DVMVNGKGAF FCDLVLIYLI KKREFYRDKK YEEVRGLEDS
     SQEAEDEASG LGLSEQLTSG PGLLGMPEQQ ELQEPPEAKR GSSSQKGNGS VCPQLLEPHR
     ST
//