ID   ADA28_HUMAN             Reviewed;         775 AA.
AC   Q9UKQ2; B2RMV5; Q9Y339; Q9Y3S0;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   24-JAN-2024, entry version 199.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28;
DE            Short=ADAM 28;
DE            EC=3.4.24.-;
DE   AltName: Full=Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
DE            Short=eMDC II;
DE   AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L;
DE            Short=MDC-L;
DE   Flags: Precursor;
GN   Name=ADAM28; Synonyms=ADAM23, MDCL;
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] (ISOFORMS 1 AND 2), AND VARIANT MET-765.
RC   TISSUE=Lymph node;
RX   PubMed=10506182; DOI=10.1074/jbc.274.41.29251;
RA   Roberts C.M., Tani P.H., Bridges L.C., Laszik Z., Bowditch R.D.;
RT   "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family
RT   member expressed by human lymphocytes.";
RL   J. Biol. Chem. 274:29251-29259(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-765.
RC   TISSUE=Epididymis;
RX   PubMed=10587367; DOI=10.1093/molehr/5.12.1127;
RA   Jury J.A., Perry A.C., Hall L.;
RT   "Identification, sequence analysis and expression of transcripts encoding a
RT   putative metalloproteinase, eMDC II, in human and macaque epididymis.";
RL   Mol. Hum. Reprod. 5:1127-1134(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-765.
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-765.
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   [6]
RP   VARIANTS GLU-65; GLU-134; GLU-450; PHE-482 AND ASP-502.
RX   PubMed=21618342; DOI=10.1002/humu.21477;
RA   Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U.,
RA   Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT   "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and
RT   ADAM7 are often mutated in melanoma.";
RL   Hum. Mutat. 32:E2148-E2175(2011).
CC   -!- FUNCTION: May play a role in the adhesive and proteolytic events that
CC       occur during lymphocyte emigration or may function in ectodomain
CC       shedding of lymphocyte surface target proteins, such as FASL and CD40L.
CC       May be involved in sperm maturation.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- INTERACTION:
CC       Q9UKQ2; P00749: PLAU; NbExp=3; IntAct=EBI-1384181, EBI-3905042;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=MDC-LM;
CC         IsoId=Q9UKQ2-1; Sequence=Displayed;
CC       Name=2; Synonyms=MDC-LS;
CC         IsoId=Q9UKQ2-2; Sequence=VSP_005486, VSP_005487;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in secondary lymphoid
CC       tissues, such as lymph node, spleen, small intestine, stomach, colon,
CC       appendix and trachea. The lymphocyte population is responsible for
CC       expression of this protein in these tissues. Isoform 2 is expressed
CC       preferentially in spleen.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
CC   -!- PTM: Pro-domain removal and maturation may be, at least in part,
CC       autocatalytic. {ECO:0000250}.
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DR   EMBL; AF137334; AAD25099.1; -; mRNA.
DR   EMBL; AF137335; AAD25100.1; -; mRNA.
DR   EMBL; AJ242015; CAB42085.1; -; mRNA.
DR   EMBL; AC044891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63609.1; -; Genomic_DNA.
DR   EMBL; BC136478; AAI36479.1; -; mRNA.
DR   CCDS; CCDS34865.1; -. [Q9UKQ2-1]
DR   CCDS; CCDS47830.1; -. [Q9UKQ2-2]
DR   RefSeq; NP_001291280.1; NM_001304351.1.
DR   RefSeq; NP_055080.2; NM_014265.5. [Q9UKQ2-1]
DR   RefSeq; NP_068547.2; NM_021777.4. [Q9UKQ2-2]
DR   AlphaFoldDB; Q9UKQ2; -.
DR   SMR; Q9UKQ2; -.
DR   BioGRID; 116072; 5.
DR   IntAct; Q9UKQ2; 1.
DR   STRING; 9606.ENSP00000265769; -.
DR   DrugBank; DB08733; (2R,3R)-N^1^-[(1S)-2,2-DIMETHYL-1-(METHYLCARBAMOYL)PROPYL]-N^4^-HYDROXY-2-(2-METHYLPROPYL)-3-{[(1,3-THIAZOL-2-YLCARBONYL)AMINO]METHYL}BUTANEDIAMIDE.
DR   DrugBank; DB02996; 2-(Thiomethylene)-4-Methylpentanoic Acid.
DR   DrugBank; DB03880; Batimastat.
DR   DrugBank; DB02215; Furoyl-Leucine.
DR   DrugBank; DB02255; Ilomastat.
DR   DrugBank; DB02046; N-[(Furan-2-Yl)Carbonyl]-(S)-Leucyl-(R)-[1-Amino-2(1h-Indol-3-Yl)Ethyl]-Phosphonic Acid.
DR   DrugBank; DB03088; Pidolic acid.
DR   MEROPS; M12.224; -.
DR   TCDB; 8.A.77.1.3; the sheddase (sheddase) family.
DR   GlyCosmos; Q9UKQ2; 5 sites, No reported glycans.
DR   GlyGen; Q9UKQ2; 6 sites.
DR   iPTMnet; Q9UKQ2; -.
DR   PhosphoSitePlus; Q9UKQ2; -.
DR   BioMuta; ADAM28; -.
DR   DMDM; 317373485; -.
DR   jPOST; Q9UKQ2; -.
DR   MassIVE; Q9UKQ2; -.
DR   PaxDb; 9606-ENSP00000265769; -.
DR   PeptideAtlas; Q9UKQ2; -.
DR   ProteomicsDB; 84834; -. [Q9UKQ2-1]
DR   ProteomicsDB; 84835; -. [Q9UKQ2-2]
DR   Antibodypedia; 58742; 272 antibodies from 24 providers.
DR   DNASU; 10863; -.
DR   Ensembl; ENST00000265769.9; ENSP00000265769.4; ENSG00000042980.14. [Q9UKQ2-1]
DR   Ensembl; ENST00000437154.6; ENSP00000393699.2; ENSG00000042980.14. [Q9UKQ2-2]
DR   GeneID; 10863; -.
DR   KEGG; hsa:10863; -.
DR   MANE-Select; ENST00000265769.9; ENSP00000265769.4; NM_014265.6; NP_055080.2.
DR   UCSC; uc003xdx.4; human. [Q9UKQ2-1]
DR   AGR; HGNC:206; -.
DR   CTD; 10863; -.
DR   DisGeNET; 10863; -.
DR   GeneCards; ADAM28; -.
DR   HGNC; HGNC:206; ADAM28.
DR   HPA; ENSG00000042980; Group enriched (epididymis, stomach).
DR   MIM; 606188; gene.
DR   neXtProt; NX_Q9UKQ2; -.
DR   OpenTargets; ENSG00000042980; -.
DR   PharmGKB; PA24523; -.
DR   VEuPathDB; HostDB:ENSG00000042980; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000156716; -.
DR   HOGENOM; CLU_012714_7_1_1; -.
DR   InParanoid; Q9UKQ2; -.
DR   OMA; CKANDAM; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q9UKQ2; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q9UKQ2; -.
DR   SignaLink; Q9UKQ2; -.
DR   BioGRID-ORCS; 10863; 12 hits in 1155 CRISPR screens.
DR   ChiTaRS; ADAM28; human.
DR   GeneWiki; ADAM28; -.
DR   GenomeRNAi; 10863; -.
DR   Pharos; Q9UKQ2; Tbio.
DR   PRO; PR:Q9UKQ2; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9UKQ2; Protein.
DR   Bgee; ENSG00000042980; Expressed in corpus epididymis and 171 other cell types or tissues.
DR   ExpressionAtlas; Q9UKQ2; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9UKQ2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..198
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029128"
FT   CHAIN           199..775
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 28"
FT                   /id="PRO_0000029129"
FT   TOPO_DOM        199..665
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        666..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        687..775
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          204..399
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          407..493
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          625..657
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          690..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           167..174
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        690..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        315..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        354..378
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        465..485
FT                   /evidence="ECO:0000250"
FT   DISULFID        629..639
FT                   /evidence="ECO:0000250"
FT   DISULFID        633..645
FT                   /evidence="ECO:0000250"
FT   DISULFID        647..656
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         524..540
FT                   /note="TEVADKSCYNRNEGGSK -> RRTNPFPCACAKENHFR (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:10506182"
FT                   /id="VSP_005486"
FT   VAR_SEQ         541..775
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10506182"
FT                   /id="VSP_005487"
FT   VARIANT         65
FT                   /note="G -> E (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066317"
FT   VARIANT         134
FT                   /note="G -> E (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267601860)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066318"
FT   VARIANT         219
FT                   /note="R -> M (in dbSNP:rs9314282)"
FT                   /id="VAR_057067"
FT   VARIANT         226
FT                   /note="E -> D (in dbSNP:rs17736699)"
FT                   /id="VAR_057068"
FT   VARIANT         450
FT                   /note="G -> E (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267601862)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066319"
FT   VARIANT         482
FT                   /note="S -> F (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066320"
FT   VARIANT         493
FT                   /note="N -> S (in dbSNP:rs7001647)"
FT                   /id="VAR_057069"
FT   VARIANT         502
FT                   /note="G -> D (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267601864)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066321"
FT   VARIANT         593
FT                   /note="T -> K (in dbSNP:rs36041430)"
FT                   /id="VAR_057070"
FT   VARIANT         604
FT                   /note="T -> P (in dbSNP:rs35617826)"
FT                   /id="VAR_057071"
FT   VARIANT         684
FT                   /note="M -> I (in dbSNP:rs7829965)"
FT                   /id="VAR_057072"
FT   VARIANT         765
FT                   /note="V -> M (in dbSNP:rs7814768)"
FT                   /evidence="ECO:0000269|PubMed:10506182,
FT                   ECO:0000269|PubMed:10587367, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_024596"
FT   CONFLICT        513
FT                   /note="Q -> R (in Ref. 1; AAD25099/AAD25100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        774
FT                   /note="K -> E (in Ref. 1; AAD25099)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   775 AA;  87148 MW;  895E0985840F971C CRC64;
     MLQGLLPVSL LLSVAVSAIK ELPGVKKYEV VYPIRLHPLH KREAKEPEQQ EQFETELKYK
     MTINGKIAVL YLKKNKNLLA PGYTETYYNS TGKEITTSPQ IMDDCYYQGH ILNEKVSDAS
     ISTCRGLRGY FSQGDQRYFI EPLSPIHRDG QEHALFKYNP DEKNYDSTCG MDGVLWAHDL
     QQNIALPATK LVKLKDRKVQ EHEKYIEYYL VLDNGEFKRY NENQDEIRKR VFEMANYVNM
     LYKKLNTHVA LVGMEIWTDK DKIKITPNAS FTLENFSKWR GSVLSRRKRH DIAQLITATE
     LAGTTVGLAF MSTMCSPYSV GVVQDHSDNL LRVAGTMAHE MGHNFGMFHD DYSCKCPSTI
     CVMDKALSFY IPTDFSSCSR LSYDKFFEDK LSNCLFNAPL PTDIISTPIC GNQLVEMGED
     CDCGTSEECT NICCDAKTCK IKATFQCALG ECCEKCQFKK AGMVCRPAKD ECDLPEMCNG
     KSGNCPDDRF QVNGFPCHHG KGHCLMGTCP TLQEQCTELW GPGTEVADKS CYNRNEGGSK
     YGYCRRVDDT LIPCKANDTM CGKLFCQGGS DNLPWKGRIV TFLTCKTFDP EDTSQEIGMV
     ANGTKCGDNK VCINAECVDI EKAYKSTNCS SKCKGHAVCD HELQCQCEEG WIPPDCDDSS
     VVFHFSIVVG VLFPMAVIFV VVAMVIRHQS SREKQKKDQR PLSTTGTRPH KQKRKPQMVK
     AVQPQEMSQM KPHVYDLPVE GNEPPASFHK DTNALPPTVF KDNPVSTPKD SNPKA
//