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   27-MAR-2024, entry version 170.
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; 15.
DR   ComplexPortal; CPX-2461; Synaptonemal complex.
DR   IntAct; Q15431; 6.
DR   MINT; Q15431; -.
DR   STRING; 9606.ENSP00000358535; -.
DR   GlyGen; Q15431; 3 sites, 1 O-linked glycan (3 sites).
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; 9606-ENSP00000358535; -.
DR   PeptideAtlas; Q15431; -.
DR   ProteomicsDB; 60589; -.
DR   Antibodypedia; 20167; 246 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   AGR; HGNC:11487; -.
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; KHKDQYD; -.
DR   OrthoDB; 5323676at2759; -.
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; 24 hits in 1150 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 84 other cell types or tissues.
DR   ExpressionAtlas; Q15431; baseline and differential.
DR   GO; GO:0030849; C:autosome; IEA:Ensembl.
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; SYNAPTONEMAL COMPLEX PROTEIN 1; 1.
DR   PANTHER; PTHR46918:SF1; SYNAPTONEMAL COMPLEX PROTEIN 1; 1.
DR   Pfam; PF05483; SCP-1; 1.
DR   Genevisible; Q15431; HS.
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
FT                   self-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
FT                   self-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
FT                   self-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
//