SHCBP_HUMAN
ID SHCBP_HUMAN Reviewed; 672 AA.
AC Q8NEM2; Q96N60; Q9BVS0; Q9H6P6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=SHC SH2 domain-binding protein 1;
GN Name=SHCBP1;
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 [LARGE SCALE MRNA], AND VARIANT THR-21.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-21.
RC TISSUE=Placenta, and Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, VARIANT [LARGE SCALE
RP ANALYSIS] THR-21, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-42; SER-44; SER-47;
RP SER-273 AND SER-634, VARIANT [LARGE SCALE ANALYSIS] THR-21, AND
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH KIF23 AND RACGAP1, AND SUBCELLULAR LOCATION.
RX PubMed=21187330; DOI=10.1083/jcb.201007060;
RA Montembault E., Zhang W., Przewloka M.R., Archambault V., Sevin E.W.,
RA Laue E.D., Glover D.M., D'Avino P.P.;
RT "Nessun Dorma, a novel centralspindlin partner, is required for cytokinesis
RT in Drosophila spermatocytes.";
RL J. Cell Biol. 191:1351-1365(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5; THR-7; SER-31 AND SER-634, VARIANT [LARGE SCALE
RP ANALYSIS] THR-21, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS],
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-31 AND SER-42, VARIANT
RP [LARGE SCALE ANALYSIS] THR-21, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: May play a role in signaling pathways governing cellular
CC proliferation, cell growth and differentiation. May be a component of a
CC novel signaling pathway downstream of Shc. Acts as a positive regulator
CC of FGF signaling in neural progenitor cells.
CC {ECO:0000250|UniProtKB:Q9Z179}.
CC -!- SUBUNIT: Interacts directly with isoform p52shc of SHC1 via its SH2
CC domain (By similarity). Interacts with TRIM71; leading to enhanced
CC SHCBP1 protein stability (By similarity). Interacts with both members
CC of the centralspindlin complex, KIF23 and RACGAP1 (PubMed:21187330).
CC {ECO:0000250|UniProtKB:Q9Z179, ECO:0000269|PubMed:21187330}.
CC -!- INTERACTION:
CC Q8NEM2; P05771: PRKCB; NbExp=3; IntAct=EBI-744700, EBI-706216;
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000269|PubMed:21187330}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:21187330}. Note=Displays weak
CC localization to the spindle midzone in some early telophase cells and
CC is concentrated at the midbody in late cytokinesis.
CC {ECO:0000269|PubMed:21187330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15208.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK025662; BAB15208.1; ALT_INIT; mRNA.
DR EMBL; AK055931; BAB71049.1; -; mRNA.
DR EMBL; AC092368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000960; AAH00960.1; -; mRNA.
DR EMBL; BC030699; AAH30699.1; -; mRNA.
DR CCDS; CCDS10720.1; -.
DR RefSeq; NP_079021.3; NM_024745.4.
DR AlphaFoldDB; Q8NEM2; -.
DR SMR; Q8NEM2; -.
DR BioGRID; 122898; 65.
DR CORUM; Q8NEM2; -.
DR IntAct; Q8NEM2; 32.
DR MINT; Q8NEM2; -.
DR STRING; 9606.ENSP00000306473; -.
DR iPTMnet; Q8NEM2; -.
DR PhosphoSitePlus; Q8NEM2; -.
DR BioMuta; SHCBP1; -.
DR DMDM; 296452958; -.
DR EPD; Q8NEM2; -.
DR jPOST; Q8NEM2; -.
DR MassIVE; Q8NEM2; -.
DR MaxQB; Q8NEM2; -.
DR PaxDb; Q8NEM2; -.
DR PeptideAtlas; Q8NEM2; -.
DR PRIDE; Q8NEM2; -.
DR ProteomicsDB; 73181; -.
DR Antibodypedia; 43856; 120 antibodies from 20 providers.
DR DNASU; 79801; -.
DR Ensembl; ENST00000303383.8; ENSP00000306473.3; ENSG00000171241.9.
DR GeneID; 79801; -.
DR KEGG; hsa:79801; -.
DR MANE-Select; ENST00000303383.8; ENSP00000306473.3; NM_024745.5; NP_079021.4.
DR UCSC; uc002eec.5; human.
DR CTD; 79801; -.
DR DisGeNET; 79801; -.
DR GeneCards; SHCBP1; -.
DR HGNC; HGNC:29547; SHCBP1.
DR HPA; ENSG00000171241; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 611027; gene.
DR neXtProt; NX_Q8NEM2; -.
DR OpenTargets; ENSG00000171241; -.
DR PharmGKB; PA134931125; -.
DR VEuPathDB; HostDB:ENSG00000171241; -.
DR eggNOG; ENOG502QUQ2; Eukaryota.
DR GeneTree; ENSGT00940000161310; -.
DR HOGENOM; CLU_022717_2_0_1; -.
DR InParanoid; Q8NEM2; -.
DR OMA; KIEPAGW; -.
DR OrthoDB; 1276823at2759; -.
DR PhylomeDB; Q8NEM2; -.
DR TreeFam; TF329196; -.
DR PathwayCommons; Q8NEM2; -.
DR SignaLink; Q8NEM2; -.
DR BioGRID-ORCS; 79801; 17 hits in 1082 CRISPR screens.
DR ChiTaRS; SHCBP1; human.
DR GeneWiki; SHCBP1; -.
DR GenomeRNAi; 79801; -.
DR Pharos; Q8NEM2; Tbio.
DR PRO; PR:Q8NEM2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NEM2; protein.
DR Bgee; ENSG00000171241; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q8NEM2; baseline and differential.
DR Genevisible; Q8NEM2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045140; SHCBP1-like.
DR PANTHER; PTHR14695; PTHR14695; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..672
FT /note="SHC SH2 domain-binding protein 1"
FT /id="PRO_0000076315"
FT REPEAT 428..451
FT /note="PbH1 1"
FT REPEAT 452..473
FT /note="PbH1 2"
FT REPEAT 474..496
FT /note="PbH1 3"
FT REPEAT 497..518
FT /note="PbH1 4"
FT REPEAT 526..548
FT /note="PbH1 5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VARIANT 21
FT /note="M -> T (in dbSNP:rs6598679)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_051354"
FT VARIANT 60
FT /note="M -> R (in dbSNP:rs11545690)"
FT /id="VAR_051355"
FT CONFLICT 118
FT /note="V -> A (in Ref. 1; BAB71049)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="Q -> R (in Ref. 1; BAB71049)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="K -> R (in Ref. 1; BAB15208)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> A (in Ref. 1; BAB15208)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="N -> S (in Ref. 3; AAH30699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 75690 MW; F3BF0210D5413376 CRC64;
MADGSLTGGG LEAAAMAPER MGWAVEQELA SLEKGLFQDE DSCSDCSYRD KPGSSLQSFM
PEGKTFFPEI FQTNQLLFYE RFRAYQDYIL ADCKASEVQE FTAEFLEKVL EPSGWRAVWH
TNVFKVLVEI TDVDFAALKA VVRLAEPYLC DSQVSTFTME CMKELLDLKE HRLPLQELWV
VFDDSGVFDQ TALAIEHVRF FYQNIWRSWD EEEEDEYDYF VRCVEPRLRL HYDILEDRVP
SGLIVDYHNL LSQCEESYRK FLNLRSSLSN CNSDSEQENI SMVEGLKLYS EMEQLKQKLK
LIENPLLRYV FGYQKNSNIQ AKGVRSSGQK ITHVVSSTMM AGLLRSLLTD RLCQEPGEEE
REIQFHSDPL SAINACFEGD TVIVCPGHYV VHGTFSIADS IELEGYGLPD DIVIEKRGKG
DTFVDCTGAD IKISGIKFVQ HDAVEGILIV HRGKTTLENC VLQCETTGVT VRTSAEFLMK
NSDLYGAKGA GIEIYPGSQC TLSDNGIHHC KEGILIKDFL DEHYDIPKIS MVNNIIHNNE
GYGVVLVKPT IFSDLQENAE DGTEENKALK IQTSGEPDVA ERVDLEELIE CATGKMELCA
RTDPSEQVEG NCEIVNELIA ASTQKGQIKK KRLSELGITQ ADDNLMSQEM FVGIVGNQFK
WNGKGSFGTF LF
