SYCP1_HUMAN
ID SYCP1_HUMAN Reviewed; 976 AA.
AC Q15431; O14963; Q5VXJ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Synaptonemal complex protein 1 {ECO:0000303|PubMed:9119375};
DE Short=SCP-1;
DE AltName: Full=Cancer/testis antigen 8;
DE Short=CT8;
GN Name=SYCP1 {ECO:0000303|PubMed:29915389, ECO:0000312|HGNC:HGNC:11487};
GN Synonyms=SCP1 {ECO:0000303|PubMed:9371398};
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 VARIANT ASP-805.
RC TISSUE=Testis;
RX PubMed=9119375; DOI=10.1006/geno.1996.4373;
RA Meuwissen R.L.J., Meerts I., Hoovers J.M.N., Leschot N.J., Heyting C.;
RT "Human synaptonemal complex protein 1 (SCP1): isolation and
RT characterization of the cDNA and chromosomal localization of the gene.";
RL Genomics 39:377-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9371398; DOI=10.1159/000134637;
RA Kondoh N., Nishina Y., Tsuchida J., Koga M., Tanaka H., Uchida K.,
RA Inazawa J., Taketo M., Nozaki M., Nojima H., Matsumiya K., Namiki M.,
RA Okuyama A., Nishimune Y.;
RT "Assignment of synaptonemal complex protein 1 (SCP1) to human chromosome
RT 1p13 by fluorescence in situ hybridization and its expression in the
RT testis.";
RL Cytogenet. Cell Genet. 78:103-104(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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].
RC TISSUE=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 [6]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=26323297; DOI=10.1107/s2053230x15012728;
RA Park H.H.;
RT "X-ray crystallographic studies of the middle part of the human
RT synaptonemal complex protein 1 coiled-coil domain.";
RL Acta Crystallogr. F 71:1131-1134(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 101-206, X-RAY CRYSTALLOGRAPHY
RP (2.15 ANGSTROMS) OF 676-770, MUTAGENESIS OF 101-GLY--LYS-111; VAL-105;
RP LEU-109; LEU-679; ILE-688; HIS-717 AND TYR-721, REGION, SUBUNIT, DOMAIN,
RP AND MOTIF.
RX PubMed=29915389; DOI=10.1038/s41594-018-0078-9;
RA Dunce J.M., Dunne O.M., Ratcliff M., Millan C., Madgwick S., Uson I.,
RA Davies O.R.;
RT "Structural basis of meiotic chromosome synapsis through SYCP1 self-
RT assembly.";
RL Nat. Struct. Mol. Biol. 25:557-569(2018).
CC -!- FUNCTION: Major component of the transverse filaments of synaptonemal
CC complexes, formed between homologous chromosomes during meiotic
CC prophase. Required for normal assembly of the central element of the
CC synaptonemal complexes. Required for normal centromere pairing during
CC meiosis. Required for normal meiotic chromosome synapsis during oocyte
CC and spermatocyte development and for normal male and female fertility.
CC {ECO:0000250|UniProtKB:Q62209}.
CC -!- SUBUNIT: Structural component of synaptonemal complexes (By
CC similarity). Homotetramer that consists of an N-terminal four-helical
CC bundle that bifurcates into two elongated C-terminal dimeric coiled
CC coils (PubMed:29915389, PubMed:26323297). This tetrameric building
CC block potentially self-assembles into a supramolecular zipper-like
CC lattice to mediate meiotic chromosome synapsis. Self-assembly is likely
CC initiated by local proton density at chromosome axis, which is
CC predicted to trigger antiparallel back to back assembly of adjacent C-
CC terminal ends into tetrameric structures that anchor to chromosomal
CC DNA. Then the N-terminal ends are predicted to undergo cooperative
CC antiparallel head to head assembly at the midline of synaptonemal
CC complexes central element to form a zipper-like lattice between
CC properly aligned homologous chromosomes (PubMed:29915389). The nascent
CC synapsis generated by SYCP1 is stabilized through interaction with
CC central element proteins SYCE1 and SYCE2 (By similarity). Forms a
CC complex with EWSR1, PRDM9, SYCP3 and REC8; complex formation is
CC dependent of phosphorylated form of REC8 and requires PRDM9 bound to
CC hotspot DNA; EWSR1 joins PRDM9 with the chromosomal axis through REC8
CC (By similarity). Interacts with SPO16 (By similarity).
CC {ECO:0000250|UniProtKB:Q62209, ECO:0000269|PubMed:26323297,
CC ECO:0000269|PubMed:29915389}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62209}.
CC Chromosome {ECO:0000250|UniProtKB:Q62209}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q62209}. Note=In tripartite segments of
CC synaptonemal complexes, between lateral elements in the nucleus. Its N-
CC terminus is found towards the center of the synaptonemal complex while
CC the C-terminus extends well into the lateral domain of the synaptonemal
CC complex (By similarity). Only rarely detected at centromeres during
CC leptotene and zygotene. Detected at centromeres during mid-diplotene,
CC when it is no longer present along chromosome arms. No longer detected
CC at centromeres at later stages of meiosis (By similarity).
CC {ECO:0000250|UniProtKB:Q03410, ECO:0000250|UniProtKB:Q62209}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:9371398}.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 4
CC polypeptide chains. The N-terminal and C-terminal regions exhibit a
CC prominent seven-residues periodicity. {ECO:0000269|PubMed:29915389}.
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DR EMBL; X95654; CAA64956.1; -; mRNA.
DR EMBL; D67035; BAA22586.1; -; mRNA.
DR EMBL; AL645502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56622.1; -; Genomic_DNA.
DR EMBL; BC126266; AAI26267.1; -; mRNA.
DR CCDS; CCDS879.1; -.
DR RefSeq; NP_001269470.1; NM_001282541.1.
DR RefSeq; NP_003167.2; NM_003176.3.
DR RefSeq; XP_006710922.1; XM_006710859.1.
DR RefSeq; XP_016857673.1; XM_017002184.1.
DR PDB; 4YTO; X-ray; 2.00 A; A/B=662-801.
DR PDB; 6F5X; X-ray; 1.91 A; A=101-175.
DR PDB; 6F62; X-ray; 2.07 A; A/B=101-206.
DR PDB; 6F63; X-ray; 2.15 A; A/B/C/D=676-770.
DR PDB; 6F64; X-ray; 2.49 A; A=676-770.
DR PDBsum; 4YTO; -.
DR PDBsum; 6F5X; -.
DR PDBsum; 6F62; -.
DR PDBsum; 6F63; -.
DR PDBsum; 6F64; -.
DR AlphaFoldDB; Q15431; -.
DR SMR; Q15431; -.
DR BioGRID; 112714; 14.
DR IntAct; Q15431; 6.
DR MINT; Q15431; -.
DR STRING; 9606.ENSP00000358535; -.
DR iPTMnet; Q15431; -.
DR PhosphoSitePlus; Q15431; -.
DR SwissPalm; Q15431; -.
DR BioMuta; SYCP1; -.
DR DMDM; 209572682; -.
DR EPD; Q15431; -.
DR MassIVE; Q15431; -.
DR MaxQB; Q15431; -.
DR PaxDb; Q15431; -.
DR PeptideAtlas; Q15431; -.
DR PRIDE; Q15431; -.
DR ProteomicsDB; 60589; -.
DR Antibodypedia; 20167; 231 antibodies from 25 providers.
DR DNASU; 6847; -.
DR Ensembl; ENST00000369518.1; ENSP00000358531.1; ENSG00000198765.12.
DR Ensembl; ENST00000369522.8; ENSP00000358535.3; ENSG00000198765.12.
DR Ensembl; ENST00000618516.4; ENSP00000480997.1; ENSG00000198765.12.
DR GeneID; 6847; -.
DR KEGG; hsa:6847; -.
DR MANE-Select; ENST00000369522.8; ENSP00000358535.3; NM_003176.4; NP_003167.2.
DR UCSC; uc001efq.5; human.
DR CTD; 6847; -.
DR DisGeNET; 6847; -.
DR GeneCards; SYCP1; -.
DR HGNC; HGNC:11487; SYCP1.
DR HPA; ENSG00000198765; Tissue enriched (testis).
DR MIM; 602162; gene.
DR neXtProt; NX_Q15431; -.
DR OpenTargets; ENSG00000198765; -.
DR PharmGKB; PA36269; -.
DR VEuPathDB; HostDB:ENSG00000198765; -.
DR eggNOG; ENOG502QTHX; Eukaryota.
DR GeneTree; ENSGT00390000003368; -.
DR InParanoid; Q15431; -.
DR OMA; RLEMCFK; -.
DR OrthoDB; 286986at2759; -.
DR PhylomeDB; Q15431; -.
DR TreeFam; TF331737; -.
DR PathwayCommons; Q15431; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR SignaLink; Q15431; -.
DR SIGNOR; Q15431; -.
DR BioGRID-ORCS; 6847; 23 hits in 1072 CRISPR screens.
DR ChiTaRS; SYCP1; human.
DR GeneWiki; SYCP1; -.
DR GenomeRNAi; 6847; -.
DR Pharos; Q15431; Tbio.
DR PRO; PR:Q15431; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15431; protein.
DR Bgee; ENSG00000198765; Expressed in sperm and 82 other tissues.
DR ExpressionAtlas; Q15431; baseline and differential.
DR Genevisible; Q15431; HS.
DR GO; GO:0000801; C:central element; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0001673; C:male germ cell nucleus; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; ISS:UniProtKB.
DR GO; GO:0000802; C:transverse filament; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0051878; P:lateral element assembly; IBA:GO_Central.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0035092; P:sperm DNA condensation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
DR InterPro; IPR008827; SYCP1.
DR PANTHER; PTHR46918; PTHR46918; 1.
DR Pfam; PF05483; SCP-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; DNA-binding; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..976
FT /note="Synaptonemal complex protein 1"
FT /id="PRO_0000072362"
FT REGION 676..770
FT /note="Required for pH-induced assembly of C-terminal ends
FT into antiparallel tetramers"
FT /evidence="ECO:0000269|PubMed:29915389"
FT REGION 784..976
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:29915389"
FT COILED 211..316
FT /evidence="ECO:0000255"
FT COILED 391..439
FT /evidence="ECO:0000255"
FT COILED 499..685
FT /evidence="ECO:0000255"
FT COILED 739..798
FT /evidence="ECO:0000255, ECO:0000269|PubMed:29915389"
FT MOTIF 101..111
FT /note="Mediates head to head self-assembly of N-terminal
FT ends"
FT /evidence="ECO:0000269|PubMed:29915389"
FT MOTIF 117..120
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 679..682
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 880..883
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VARIANT 78
FT /note="E -> D (in dbSNP:rs12563933)"
FT /id="VAR_046993"
FT VARIANT 805
FT /note="E -> D (in dbSNP:rs1053812)"
FT /evidence="ECO:0000269|PubMed:9119375"
FT /id="VAR_046994"
FT MUTAGEN 101..111
FT /note="Missing: Impairs self-assembly of N-terminal ends."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 105
FT /note="V->E: Impairs self-assembly of N-terminal ends; when
FT associated with E-109."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 109
FT /note="L->E: Impairs self-assembly of N-terminal ends; when
FT associated with E-105."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 679
FT /note="L->A: Impairs pH-induced C-terminal tetrameric self-
FT assembly; when associated with A-688."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 688
FT /note="I->A: Impairs pH-induced C-terminal tetrameric self-
FT assembly; when associated with A-679."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 717
FT /note="H->E: Impairs pH-induced C-terminal tetrameric self-
FT assembly."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 717
FT /note="H->W: Enables C-terminal tetrameric self-assembly at
FT pH 8.0; when associated with F-721."
FT /evidence="ECO:0000269|PubMed:29915389"
FT MUTAGEN 721
FT /note="Y->F: Enables C-terminal tetrameric self-assembly at
FT pH 8.0; when associated with W-717."
FT /evidence="ECO:0000269|PubMed:29915389"
FT CONFLICT 46
FT /note="F -> L (in Ref. 1; CAA64956)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Y -> F (in Ref. 1; CAA64956)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="F -> C (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="K -> T (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="E -> D (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="N -> S (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..226
FT /note="FE -> HG (in Ref. 1; CAA64956)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="K -> N (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="E -> D (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="KN -> NY (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="K -> I (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="K -> T (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="E -> D (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 483..510
FT /note="IQLTAITTSEQYYSKEVKDLKTELENEK -> YSYCHYHKWTVLPKRGQRPK
FT LSSKRE (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 516..528
FT /note="LTSHCNKLSLENK -> YFTLQQASPPPN (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="N -> I (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="K -> T (in Ref. 2; BAA22586)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="S -> P (in Ref. 1; CAA64956)"
FT /evidence="ECO:0000305"
FT HELIX 101..170
FT /evidence="ECO:0007829|PDB:6F5X"
FT HELIX 675..726
FT /evidence="ECO:0007829|PDB:4YTO"
FT HELIX 728..765
FT /evidence="ECO:0007829|PDB:4YTO"
SQ SEQUENCE 976 AA; 114192 MW; 43058F1A4B7F57E5 CRC64;
MEKQKPFALF VPPRSSSSQV SAVKPQTLGG DSTFFKSFNK CTEDDFEFPF AKTNLSKNGE
NIDSDPALQK VNFLPVLEQV GNSDCHYQEG LKDSDLENSE GLSRVYSKLY KEAEKIKKWK
VSTEAELRQK ESKLQENRKI IEAQRKAIQE LQFGNEKVSL KLEEGIQENK DLIKENNATR
HLCNLLKETC ARSAEKTKKY EYEREETRQV YMDLNNNIEK MITAFEELRV QAENSRLEMH
FKLKEDYEKI QHLEQEYKKE INDKEKQVSL LLIQITEKEN KMKDLTFLLE ESRDKVNQLE
EKTKLQSENL KQSIEKQHHL TKELEDIKVS LQRSVSTQKA LEEDLQIATK TICQLTEEKE
TQMEESNKAR AAHSFVVTEF ETTVCSLEEL LRTEQQRLEK NEDQLKILTM ELQKKSSELE
EMTKLTNNKE VELEELKKVL GEKETLLYEN KQFEKIAEEL KGTEQELIGL LQAREKEVHD
LEIQLTAITT SEQYYSKEVK DLKTELENEK LKNTELTSHC NKLSLENKEL TQETSDMTLE
LKNQQEDINN NKKQEERMLK QIENLQETET QLRNELEYVR EELKQKRDEV KCKLDKSEEN
CNNLRKQVEN KNKYIEELQQ ENKALKKKGT AESKQLNVYE IKVNKLELEL ESAKQKFGEI
TDTYQKEIED KKISEENLLE EVEKAKVIAD EAVKLQKEID KRCQHKIAEM VALMEKHKHQ
YDKIIEERDS ELGLYKSKEQ EQSSLRASLE IELSNLKAEL LSVKKQLEIE REEKEKLKRE
AKENTATLKE KKDKKTQTFL LETPEIYWKL DSKAVPSQTV SRNFTSVDHG ISKDKRDYLW
TSAKNTLSTP LPKAYTVKTP TKPKLQQREN LNIPIEESKK KRKMAFEFDI NSDSSETTDL
LSMVSEEETL KTLYRNNNPP ASHLCVKTPK KAPSSLTTPG STLKFGAIRK MREDRWAVIA
KMDRKKKLKE AEKLFV
