CDCA5_HUMAN
ID CDCA5_HUMAN Reviewed; 252 AA.
AC Q96FF9; A8K625;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Sororin;
DE AltName: Full=Cell division cycle-associated protein 5;
DE AltName: Full=p35;
GN Name=CDCA5;
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].
RX PubMed=12188893; DOI=10.2174/1568009013334241;
RA Walker M.G.;
RT "Drug target discovery by gene expression analysis: cell cycle genes.";
RL Curr. Cancer Drug Targets 1:73-83(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, AND
RP IDENTIFICATION IN A COMPLEX WITH SMC1A; SMC3; RAD21; PDS5A AND PDS5B.
RX PubMed=15837422; DOI=10.1016/j.molcel.2005.03.017;
RA Rankin S., Ayad N.G., Kirschner M.W.;
RT "Sororin, a substrate of the anaphase-promoting complex, is required for
RT sister chromatid cohesion in vertebrates.";
RL Mol. Cell 18:185-200(2005).
RN [6]
RP ERRATUM OF PUBMED:15837422.
RA Rankin S., Ayad N.G., Kirschner M.W.;
RL Mol. Cell 18:609-609(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP FUNCTION, AND INTERACTION WITH THE COHESIN COMPLEX.
RX PubMed=17349791; DOI=10.1016/j.cub.2007.02.029;
RA Schmitz J., Watrin E., Lenart P., Mechtler K., Peters J.M.;
RT "Sororin is required for stable binding of cohesin to chromatin and for
RT sister chromatid cohesion in interphase.";
RL Curr. Biol. 17:630-636(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-35; THR-115 AND
RP SER-209, AND 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, 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 [14]
RP FUNCTION, INTERACTION WITH PDS5A AND PDS5B, MUTAGENESIS OF
RP 166-PHE--PHE-168, AND FGF MOTIF.
RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031;
RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A.,
RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.;
RT "Sororin mediates sister chromatid cohesion by antagonizing wapl.";
RL Cell 143:737-749(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-75; SER-79 AND
RP SER-209, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-33; SER-75; SER-79;
RP SER-83; THR-98; SER-107; THR-111; SER-154 AND THR-159, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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: Regulator of sister chromatid cohesion in mitosis stabilizing
CC cohesin complex association with chromatin. May antagonize the action
CC of WAPL which stimulates cohesin dissociation from chromatin. Cohesion
CC ensures that chromosome partitioning is accurate in both meiotic and
CC mitotic cells and plays an important role in DNA repair. Required for
CC efficient DNA double-stranded break repair.
CC {ECO:0000269|PubMed:15837422, ECO:0000269|PubMed:17349791,
CC ECO:0000269|PubMed:21111234}.
CC -!- SUBUNIT: Interacts with the APC/C complex (By similarity). Interacts
CC with the chromatin-bound cohesin complex; the interaction is indirect,
CC occurs after DNA replication and requires acetylation of the cohesin
CC component SMC3. Interacts (via the FGF motif) with PDS5A and PDS5B; the
CC interaction is direct and prevents the interaction of PDS5A with WAPL.
CC {ECO:0000250, ECO:0000269|PubMed:15837422, ECO:0000269|PubMed:17349791,
CC ECO:0000269|PubMed:21111234}.
CC -!- INTERACTION:
CC Q96FF9; P41227: NAA10; NbExp=5; IntAct=EBI-718805, EBI-747693;
CC Q96FF9; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-718805, EBI-2585120;
CC Q96FF9; Q29RF7: PDS5A; NbExp=3; IntAct=EBI-718805, EBI-1175454;
CC Q96FF9; Q5FBB7: SGO1; NbExp=4; IntAct=EBI-718805, EBI-989069;
CC Q96FF9; Q14683: SMC1A; NbExp=6; IntAct=EBI-718805, EBI-80690;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15837422}. Chromosome
CC {ECO:0000269|PubMed:15837422}. Cytoplasm {ECO:0000269|PubMed:15837422}.
CC Note=Associates with nuclear chromatin from S phase until metaphase and
CC is released in the cytoplasm upon nuclear envelope breakdown.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C
CC complex. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts
CC the interaction with PDS5A and relieves the inhibition of WAPL by
CC CDCA5. {ECO:0000269|PubMed:15837422}.
CC -!- PTM: Ubiquitinated by the APC/C complex in G1, leading to its
CC degradation. {ECO:0000305|PubMed:15837422}.
CC -!- MISCELLANEOUS: Named sororin after the Latin word 'soror', which means
CC 'sister', because of its critical role in sister chromatid cohesion.
CC -!- SIMILARITY: Belongs to the sororin family. {ECO:0000305}.
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DR EMBL; BG354578; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291490; BAF84179.1; -; mRNA.
DR EMBL; CH471076; EAW74342.1; -; Genomic_DNA.
DR EMBL; BC011000; AAH11000.1; -; mRNA.
DR CCDS; CCDS8091.1; -.
DR RefSeq; NP_542399.1; NM_080668.3.
DR AlphaFoldDB; Q96FF9; -.
DR BioGRID; 125225; 135.
DR CORUM; Q96FF9; -.
DR DIP; DIP-47377N; -.
DR ELM; Q96FF9; -.
DR IntAct; Q96FF9; 52.
DR MINT; Q96FF9; -.
DR STRING; 9606.ENSP00000275517; -.
DR GlyGen; Q96FF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96FF9; -.
DR PhosphoSitePlus; Q96FF9; -.
DR BioMuta; CDCA5; -.
DR DMDM; 68565257; -.
DR EPD; Q96FF9; -.
DR jPOST; Q96FF9; -.
DR MassIVE; Q96FF9; -.
DR MaxQB; Q96FF9; -.
DR PaxDb; Q96FF9; -.
DR PeptideAtlas; Q96FF9; -.
DR PRIDE; Q96FF9; -.
DR ProteomicsDB; 76523; -.
DR Antibodypedia; 15765; 105 antibodies from 19 providers.
DR DNASU; 113130; -.
DR Ensembl; ENST00000275517.8; ENSP00000275517.3; ENSG00000146670.10.
DR GeneID; 113130; -.
DR KEGG; hsa:113130; -.
DR MANE-Select; ENST00000275517.8; ENSP00000275517.3; NM_080668.4; NP_542399.1.
DR UCSC; uc001ocp.3; human.
DR CTD; 113130; -.
DR DisGeNET; 113130; -.
DR GeneCards; CDCA5; -.
DR HGNC; HGNC:14626; CDCA5.
DR HPA; ENSG00000146670; Group enriched (bone marrow, lymphoid tissue, testis).
DR MIM; 609374; gene.
DR neXtProt; NX_Q96FF9; -.
DR OpenTargets; ENSG00000146670; -.
DR PharmGKB; PA26278; -.
DR VEuPathDB; HostDB:ENSG00000146670; -.
DR eggNOG; ENOG502S4XG; Eukaryota.
DR GeneTree; ENSGT00390000010028; -.
DR HOGENOM; CLU_088614_0_0_1; -.
DR InParanoid; Q96FF9; -.
DR OMA; KKVQQID; -.
DR OrthoDB; 961382at2759; -.
DR PhylomeDB; Q96FF9; -.
DR TreeFam; TF101070; -.
DR PathwayCommons; Q96FF9; -.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR SignaLink; Q96FF9; -.
DR SIGNOR; Q96FF9; -.
DR BioGRID-ORCS; 113130; 542 hits in 1084 CRISPR screens.
DR ChiTaRS; CDCA5; human.
DR GeneWiki; CDCA5; -.
DR GenomeRNAi; 113130; -.
DR Pharos; Q96FF9; Tbio.
DR PRO; PR:Q96FF9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96FF9; protein.
DR Bgee; ENSG00000146670; Expressed in ventricular zone and 117 other tissues.
DR ExpressionAtlas; Q96FF9; baseline and differential.
DR Genevisible; Q96FF9; HS.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; TAS:Reactome.
DR GO; GO:0000775; C:chromosome, centromeric region; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; TAS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:UniProtKB.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:UniProtKB.
DR InterPro; IPR018605; Sororin.
DR PANTHER; PTHR31092; PTHR31092; 1.
DR Pfam; PF09666; Sororin; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..252
FT /note="Sororin"
FT /id="PRO_0000089449"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 88..90
FT /note="KEN box"
FT MOTIF 166..168
FT /note="FGF motif"
FT COMPBIAS 82..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VARIANT 156
FT /note="S -> Y (in dbSNP:rs34020666)"
FT /id="VAR_050777"
FT MUTAGEN 166..168
FT /note="FGF->AGA: Alters interaction with PDS5A and PDS5B
FT and the cohesin complex."
FT /evidence="ECO:0000269|PubMed:21111234"
SQ SEQUENCE 252 AA; 27601 MW; A4CD6768D3464040 CRC64;
MSGRRTRSGG AAQRSGPRAP SPTKPLRRSQ RKSGSELPSI LPEIWPKTPS AAAVRKPIVL
KRIVAHAVEV PAVQSPRRSP RISFFLEKEN EPPGRELTKE DLFKTHSVPA TPTSTPVPNP
EAESSSKEGE LDARDLEMSK KVRRSYSRLE TLGSASTSTP GRRSCFGFEG LLGAEDLSGV
SPVVCSKLTE VPRVCAKPWA PDMTLPGISP PPEKQKRKKK KMPEILKTEL DEWAAAMNAE
FEAAEQFDLL VE
