CD5_HUMAN
ID CD5_HUMAN Reviewed; 495 AA.
AC P06127; A0N0P4; A8K9I3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=T-cell surface glycoprotein CD5;
DE AltName: Full=Lymphocyte antigen T1/Leu-1;
DE AltName: CD_antigen=CD5;
DE Flags: Precursor;
GN Name=CD5; Synonyms=LEU1;
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], AND VARIANTS ARG-461 AND VAL-471.
RX PubMed=3093892; DOI=10.1038/323346a0;
RA Jones N.H., Clabby M.L., Dialynas D.P., Huag H.-J.S., Herzenberg L.A.,
RA Strominger J.L.;
RT "Isolation of complementary DNA clones encoding the human lymphocyte
RT glycoprotein T1/Leu-1.";
RL Nature 323:346-349(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-461 AND VAL-471.
RC TISSUE=Lymphocyte;
RX PubMed=8740779; DOI=10.1111/j.1399-0039.1996.tb02551.x;
RA Calvo J., Sole J., Simarro M., Vives J., Lozano F.;
RT "Evolutionarily conserved transcription regulatory elements within the 5'-
RT flanking region of the human CD5 gene.";
RL Tissue Antigens 47:257-261(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-461 AND VAL-471.
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-224 AND ARG-461.
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-461 AND VAL-471.
RC TISSUE=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 [7]
RP INTERACTION WITH CD72/LYB-2.
RX PubMed=1711157; DOI=10.1038/351662a0;
RA van de Velde H., von Hoegen I., Luo W., Parnes J.R., Thielemans K.;
RT "The B-cell surface protein CD72/Lyb-2 is the ligand for CD5.";
RL Nature 351:662-665(1991).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-460, VARIANT
RP [LARGE SCALE ANALYSIS] ARG-461, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C.,
RA Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT "Profiling of tyrosine phosphorylation pathways in human cells using mass
RT spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453; SER-483 AND SER-485, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 270-369.
RX PubMed=17322294; DOI=10.1074/jbc.m611699200;
RA Rodamilans B., Munoz I.G., Bragado-Nilsson E., Sarrias M.R., Padilla O.,
RA Blanco F.J., Lozano F., Montoya G.;
RT "Crystal structure of the third extracellular domain of CD5 reveals the
RT fold of a group B scavenger cysteine-rich receptor domain.";
RL J. Biol. Chem. 282:12669-12677(2007).
RN [12]
RP STRUCTURE BY NMR OF 25-134, AND DISULFIDE BONDS.
RX PubMed=18339402; DOI=10.1016/j.jmb.2008.02.006;
RA Garza-Garcia A., Esposito D., Rieping W., Harris R., Briggs C., Brown M.H.,
RA Driscoll P.C.;
RT "Three-dimensional solution structure and conformational plasticity of the
RT N-terminal scavenger receptor cysteine-rich domain of human CD5.";
RL J. Mol. Biol. 378:129-144(2008).
CC -!- FUNCTION: May act as a receptor in regulating T-cell proliferation.
CC -!- SUBUNIT: Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN; this creates binding
CC sites for PTPN6/SHP-1. {ECO:0000250}.
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DR EMBL; X04391; CAA27979.1; -; mRNA.
DR EMBL; X89405; CAA61584.2; -; Genomic_DNA.
DR EMBL; AJ237927; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; AJ237928; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; AJ237929; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; AJ237930; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; AJ237931; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; AJ237932; CAA61584.2; JOINED; Genomic_DNA.
DR EMBL; EF064752; ABK41935.1; -; Genomic_DNA.
DR EMBL; AK292698; BAF85387.1; -; mRNA.
DR EMBL; AP000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027901; AAH27901.1; -; mRNA.
DR CCDS; CCDS8000.1; -.
DR PIR; A26396; A26396.
DR RefSeq; NP_001333385.1; NM_001346456.1.
DR RefSeq; NP_055022.2; NM_014207.3.
DR PDB; 2JA4; X-ray; 2.21 A; A=270-369.
DR PDB; 2JOP; NMR; -; A=25-134.
DR PDB; 2JP0; NMR; -; A=25-134.
DR PDB; 2OTT; X-ray; 2.50 A; X/Y=276-368.
DR PDBsum; 2JA4; -.
DR PDBsum; 2JOP; -.
DR PDBsum; 2JP0; -.
DR PDBsum; 2OTT; -.
DR AlphaFoldDB; P06127; -.
DR SMR; P06127; -.
DR BioGRID; 107359; 31.
DR DIP; DIP-21N; -.
DR IntAct; P06127; 4.
DR MINT; P06127; -.
DR STRING; 9606.ENSP00000342681; -.
DR ChEMBL; CHEMBL3712888; -.
DR GlyConnect; 589; 5 N-Linked glycans.
DR GlyGen; P06127; 3 sites, 8 N-linked glycans (1 site).
DR iPTMnet; P06127; -.
DR PhosphoSitePlus; P06127; -.
DR SwissPalm; P06127; -.
DR BioMuta; CD5; -.
DR DMDM; 313104090; -.
DR jPOST; P06127; -.
DR MassIVE; P06127; -.
DR MaxQB; P06127; -.
DR PaxDb; P06127; -.
DR PeptideAtlas; P06127; -.
DR PRIDE; P06127; -.
DR ProteomicsDB; 51869; -.
DR ABCD; P06127; 79 sequenced antibodies.
DR Antibodypedia; 4206; 3821 antibodies from 54 providers.
DR DNASU; 921; -.
DR Ensembl; ENST00000347785.8; ENSP00000342681.3; ENSG00000110448.11.
DR GeneID; 921; -.
DR KEGG; hsa:921; -.
DR MANE-Select; ENST00000347785.8; ENSP00000342681.3; NM_014207.4; NP_055022.2.
DR UCSC; uc009ynk.4; human.
DR CTD; 921; -.
DR DisGeNET; 921; -.
DR GeneCards; CD5; -.
DR HGNC; HGNC:1685; CD5.
DR HPA; ENSG00000110448; Tissue enhanced (lymphoid).
DR MIM; 153340; gene.
DR neXtProt; NX_P06127; -.
DR OpenTargets; ENSG00000110448; -.
DR PharmGKB; PA26224; -.
DR VEuPathDB; HostDB:ENSG00000110448; -.
DR eggNOG; ENOG502RYTM; Eukaryota.
DR GeneTree; ENSGT00390000017536; -.
DR HOGENOM; CLU_047656_0_0_1; -.
DR InParanoid; P06127; -.
DR OMA; FHRNHTA; -.
DR OrthoDB; 1017770at2759; -.
DR PhylomeDB; P06127; -.
DR TreeFam; TF329295; -.
DR PathwayCommons; P06127; -.
DR SignaLink; P06127; -.
DR SIGNOR; P06127; -.
DR BioGRID-ORCS; 921; 23 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; P06127; -.
DR GeneWiki; CD5_(protein); -.
DR GenomeRNAi; 921; -.
DR Pharos; P06127; Tbio.
DR PRO; PR:P06127; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P06127; protein.
DR Bgee; ENSG00000110448; Expressed in granulocyte and 125 other tissues.
DR ExpressionAtlas; P06127; baseline and differential.
DR Genevisible; P06127; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0008037; P:cell recognition; NAS:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
DR Gene3D; 3.10.250.10; -; 2.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR003566; Tcell_CD5.
DR PANTHER; PTHR47309; PTHR47309; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR PRINTS; PR01409; TCELLCD5.
DR SMART; SM00202; SR; 2.
DR SUPFAM; SSF56487; SSF56487; 2.
DR PROSITE; PS50287; SRCR_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT CHAIN 25..495
FT /note="T-cell surface glycoprotein CD5"
FT /id="PRO_0000033222"
FT TOPO_DOM 25..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..133
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 159..268
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 276..368
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12522270,
FT ECO:0007744|PubMed:15144186"
FT MOD_RES 453
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:12522270"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 60..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 81..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 107..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 201..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 244..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 285..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 301..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 316..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT DISULFID 342..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:18339402"
FT VARIANT 224
FT /note="P -> L (in dbSNP:rs2241002)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_020411"
FT VARIANT 461
FT /note="H -> R (in dbSNP:rs637186)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:3093892,
FT ECO:0000269|PubMed:8740779, ECO:0000269|Ref.3,
FT ECO:0007744|PubMed:12522270"
FT /id="VAR_024649"
FT VARIANT 471
FT /note="A -> V (in dbSNP:rs2229177)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3093892, ECO:0000269|PubMed:8740779,
FT ECO:0000269|Ref.3"
FT /id="VAR_058203"
FT CONFLICT 289
FT /note="V -> E (in Ref. 4; BAF85387)"
FT /evidence="ECO:0000305"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2JOP"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2JP0"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2JOP"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2JOP"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2JA4"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2JA4"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2JA4"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:2JA4"
SQ SEQUENCE 495 AA; 54578 MW; 9131AEC9683EE1D3 CRC64;
MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV YLKDGWHMVC
SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT PQSSIICYGQ LGSFSNCSHS
RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS
LGGTISYEAQ DKTQDLENFL CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ
NSSCTSLEHC FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL
CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC HELWERNSYC
KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL AYKKLVKKFR QKKQRQWIGP
TGMNQNMSFH RNHTATVRSH AENPTASHVD NEYSQPPRNS HLSAYPALEG ALHRSSMQPD
NSSDSDYDLH GAQRL
