ID   CCNA1_HUMAN             Reviewed;         465 AA.
AC   P78396; B7Z7E3; Q5T3V0; Q5U0G2; Q8IY91;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Cyclin-A1;
GN   Name=CCNA1;
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] (ISOFORM 1).
RC   TISSUE=Myeloid;
RX   PubMed=9041194;
RA   Yang R., Morosetti R., Koeffler H.P.;
RT   "Characterization of a second human cyclin A that is highly expressed in
RT   testis and in several leukemic cell lines.";
RL   Cancer Res. 57:913-920(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 55-465.
RC   TISSUE=Testis;
RA   Perkins E.L., Wood V.J., Sterling J.F., Hashem V.I., Resnick M.A.;
RT   "The human testes cyclin A1 disrupts growth and DNA damage response of a
RT   yeast replication mutant.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION.
RX   PubMed=10022926; DOI=10.1128/mcb.19.3.2400;
RA   Yang R., Mueller C., Huynh V., Fung Y.K., Yee A.S., Koeffler H.P.;
RT   "Functions of cyclin A1 in the cell cycle and its interactions with
RT   transcription factor E2F-1 and the Rb family of proteins.";
RL   Mol. Cell. Biol. 19:2400-2407(1999).
RN   [9]
RP   INTERACTION WITH INCA1 AND KLHDC9.
RX   PubMed=15159402; DOI=10.1074/jbc.m401708200;
RA   Diederichs S., Baeumer N., Ji P., Metzelder S.K., Idos G.E., Cauvet T.,
RA   Wang W., Moeller M., Pierschalski S., Gromoll J., Schrader M.G.,
RA   Koeffler H.P., Berdel W.E., Serve H., Mueller-Tidow C.;
RT   "Identification of interaction partners and substrates of the cyclin A1-
RT   CDK2 complex.";
RL   J. Biol. Chem. 279:33727-33741(2004).
RN   [10]
RP   INTERACTION WITH INCA1.
RX   PubMed=21540187; DOI=10.1074/jbc.m110.203471;
RA   Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S.,
RA   Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G.,
RA   Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.;
RT   "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1
RT   (INCA1) regulates proliferation and is repressed by oncogenic signaling.";
RL   J. Biol. Chem. 286:28210-28222(2011).
RN   [11]
RP   UBIQUITINATION, AND DEUBIQUITINATION BY USP37.
RX   PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
RA   Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
RA   Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
RT   "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
RT   promote S phase entry.";
RL   Mol. Cell 42:511-523(2011).
CC   -!- FUNCTION: May be involved in the control of the cell cycle at the G1/S
CC       (start) and G2/M (mitosis) transitions. May primarily function in the
CC       control of the germline meiotic cell cycle and additionally in the
CC       control of mitotic cell cycle in some somatic cells.
CC       {ECO:0000269|PubMed:10022926}.
CC   -!- SUBUNIT: Interacts with the CDK2 and the CDC2 protein kinases to form a
CC       serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC       substrate specificity to the complex. Does not bind CDK4 and CDK5 (in
CC       vitro). The cyclin A1-CDK2 complex interacts with transcription factor
CC       E2F-1 and RB proteins. Found in a complex with CDK2, CABLES1 and CCNE1
CC       (By similarity). Interacts with INCA1 (PubMed:15159402,
CC       PubMed:21540187). Interacts with KLHDC9 (PubMed:15159402).
CC       {ECO:0000250|UniProtKB:Q61456, ECO:0000269|PubMed:15159402,
CC       ECO:0000269|PubMed:21540187}.
CC   -!- INTERACTION:
CC       P78396; P38936: CDKN1A; NbExp=8; IntAct=EBI-375065, EBI-375077;
CC       P78396; P46527: CDKN1B; NbExp=6; IntAct=EBI-375065, EBI-519280;
CC       P78396-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-21770675, EBI-21251460;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P78396-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P78396-2; Sequence=VSP_034392;
CC       Name=3;
CC         IsoId=P78396-3; Sequence=VSP_044257;
CC   -!- TISSUE SPECIFICITY: Very high levels in testis and very low levels in
CC       brain. Also found in myeloid leukemia cell lines.
CC   -!- DEVELOPMENTAL STAGE: Expression increases in early G1 phase and reaches
CC       highest levels during the S and G2/M phases.
CC   -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-
CC       promoting complex (APC/C), leading to its degradation by the
CC       proteasome. Deubiquitinated and stabilized by USP37 enables entry into
CC       S phase. {ECO:0000269|PubMed:21596315}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/949/CCNA1";
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DR   EMBL; U66838; AAB49754.1; -; mRNA.
DR   EMBL; BT019577; AAV38384.1; -; mRNA.
DR   EMBL; AK301897; BAH13579.1; -; mRNA.
DR   EMBL; AK316392; BAH14763.1; -; mRNA.
DR   EMBL; AL359767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08565.1; -; Genomic_DNA.
DR   EMBL; CH471075; EAX08566.1; -; Genomic_DNA.
DR   EMBL; BC036346; AAH36346.1; -; mRNA.
DR   EMBL; U97680; AAB60863.1; -; mRNA.
DR   CCDS; CCDS45031.1; -. [P78396-3]
DR   RefSeq; NP_001104515.1; NM_001111045.1. [P78396-3]
DR   RefSeq; NP_001104516.1; NM_001111046.1. [P78396-3]
DR   RefSeq; NP_001104517.1; NM_001111047.1. [P78396-3]
DR   RefSeq; NP_003905.1; NM_003914.3.
DR   RefSeq; XP_011533596.1; XM_011535294.2. [P78396-3]
DR   RefSeq; XP_011533597.1; XM_011535295.2. [P78396-3]
DR   RefSeq; XP_011533598.1; XM_011535296.2. [P78396-3]
DR   AlphaFoldDB; P78396; -.
DR   SMR; P78396; -.
DR   BioGRID; 114417; 61.
DR   ComplexPortal; CPX-2003; Cyclin A1-CDK1 complex.
DR   ComplexPortal; CPX-2005; Cyclin A1-CDK2 complex.
DR   CORUM; P78396; -.
DR   ELM; P78396; -.
DR   IntAct; P78396; 16.
DR   MINT; P78396; -.
DR   STRING; 9606.ENSP00000255465; -.
DR   BindingDB; P78396; -.
DR   ChEMBL; CHEMBL2094128; -.
DR   ChEMBL; CHEMBL3038470; -.
DR   ChEMBL; CHEMBL3885548; -.
DR   ChEMBL; CHEMBL4296066; -.
DR   iPTMnet; P78396; -.
DR   PhosphoSitePlus; P78396; -.
DR   BioMuta; CCNA1; -.
DR   DMDM; 8134359; -.
DR   EPD; P78396; -.
DR   jPOST; P78396; -.
DR   MassIVE; P78396; -.
DR   MaxQB; P78396; -.
DR   PaxDb; 9606-ENSP00000255465; -.
DR   PeptideAtlas; P78396; -.
DR   ProteomicsDB; 57612; -. [P78396-1]
DR   ProteomicsDB; 57613; -. [P78396-2]
DR   ProteomicsDB; 6859; -.
DR   Antibodypedia; 4520; 607 antibodies from 37 providers.
DR   DNASU; 8900; -.
DR   Ensembl; ENST00000255465.8; ENSP00000255465.5; ENSG00000133101.10. [P78396-3]
DR   Ensembl; ENST00000440264.5; ENSP00000400666.1; ENSG00000133101.10. [P78396-3]
DR   Ensembl; ENST00000625767.2; ENSP00000486017.2; ENSG00000133101.10. [P78396-3]
DR   Ensembl; ENST00000630422.2; ENSP00000486482.1; ENSG00000133101.10. [P78396-3]
DR   GeneID; 8900; -.
DR   KEGG; hsa:8900; -.
DR   MANE-Select; ENST00000255465.8; ENSP00000255465.5; NM_001413923.1; NP_001400852.1. [P78396-3]
DR   UCSC; uc001uvr.5; human. [P78396-1]
DR   AGR; HGNC:1577; -.
DR   CTD; 8900; -.
DR   DisGeNET; 8900; -.
DR   GeneCards; CCNA1; -.
DR   HGNC; HGNC:1577; CCNA1.
DR   HPA; ENSG00000133101; Tissue enhanced (parathyroid gland, testis).
DR   MIM; 604036; gene.
DR   neXtProt; NX_P78396; -.
DR   OpenTargets; ENSG00000133101; -.
DR   PharmGKB; PA26147; -.
DR   VEuPathDB; HostDB:ENSG00000133101; -.
DR   eggNOG; KOG0654; Eukaryota.
DR   GeneTree; ENSGT00940000157940; -.
DR   InParanoid; P78396; -.
DR   OMA; YKSSKYC; -.
DR   OrthoDB; 5474295at2759; -.
DR   PhylomeDB; P78396; -.
DR   TreeFam; TF101002; -.
DR   PathwayCommons; P78396; -.
DR   Reactome; R-HSA-1538133; G0 and Early G1.
DR   Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
DR   Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-HSA-68911; G2 Phase.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR   Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
DR   Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   SignaLink; P78396; -.
DR   SIGNOR; P78396; -.
DR   BioGRID-ORCS; 8900; 11 hits in 1156 CRISPR screens.
DR   ChiTaRS; CCNA1; human.
DR   GeneWiki; Cyclin_A1; -.
DR   GenomeRNAi; 8900; -.
DR   Pharos; P78396; Tbio.
DR   PRO; PR:P78396; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; P78396; Protein.
DR   Bgee; ENSG00000133101; Expressed in sperm and 119 other cell types or tissues.
DR   ExpressionAtlas; P78396; baseline and differential.
DR   GO; GO:0097123; C:cyclin A1-CDK2 complex; IEA:Ensembl.
DR   GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007141; P:male meiosis I; TAS:ProtInc.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR   CDD; cd20560; CYCLIN_CCNA1_rpt1; 1.
DR   CDD; cd20563; CYCLIN_CCNA1_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR032447; Cyclin-A_N.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177:SF254; CYCLIN-A1; 1.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF16500; Cyclin_N2; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
DR   Genevisible; P78396; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Cyclin; Mitosis; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..465
FT                   /note="Cyclin-A1"
FT                   /id="PRO_0000080333"
FT   VAR_SEQ         1..44
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044257"
FT   VAR_SEQ         38
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_034392"
FT   CONFLICT        43..47
FT                   /note="EAMHC -> SS (in Ref. 2; AAV38384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   465 AA;  52358 MW;  C9C023EEA1CF036D CRC64;
     METGFPAIMY PGSFIGGWGE EYLSWEGPGL PDFVFQQQPV ESEAMHCSNP KSGVVLATVA
     RGPDACQILT RAPLGQDPPQ RTVLGLLTAN GQYRRTCGQG ITRIRCYSGS ENAFPPAGKK
     ALPDCGVQEP PKQGFDIYMD ELEQGDRDSC SVREGMAFED VYEVDTGTLK SDLHFLLDFN
     TVSPMLVDSS LLSQSEDISS LGTDVINVTE YAEEIYQYLR EAEIRHRPKA HYMKKQPDIT
     EGMRTILVDW LVEVGEEYKL RAETLYLAVN FLDRFLSCMS VLRGKLQLVG TAAMLLASKY
     EEIYPPEVDE FVYITDDTYT KRQLLKMEHL LLKVLAFDLT VPTTNQFLLQ YLRRQGVCVR
     TENLAKYVAE LSLLEADPFL KYLPSLIAAA AFCLANYTVN KHFWPETLAA FTGYSLSEIV
     PCLSELHKAY LDIPHRPQQA IREKYKASKY LCVSLMEPPA VLLLQ
//