ID   ADA18_HUMAN             Reviewed;         739 AA.
AC   Q9Y3Q7; B2R9Y0; Q0VAI4; Q6IRW9; Q6UXJ9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 18;
DE            Short=ADAM 18;
DE   AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein III;
DE            Short=tMDC III;
DE   Flags: Precursor;
GN   Name=ADAM18; Synonyms=TMDC3; ORFNames=UNQ858/PRO1867;
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=Testis;
RA   Hall L., Frayne J., Dimsey E.A.;
RT   "Nucleotide sequence of the human tMDC III sperm surface protein
RT   transcript.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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   VARIANTS SER-170; GLY-284; ILE-344; LYS-362 AND LEU-536.
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: Sperm surface membrane protein that may be involved in
CC       spermatogenesis and fertilization. This is a non catalytic
CC       metalloprotease-like protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y3Q7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y3Q7-2; Sequence=VSP_012033;
CC       Name=3;
CC         IsoId=Q9Y3Q7-3; Sequence=VSP_043285, VSP_043286;
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DOMAIN: A tripeptide motif (ECD) within disintegrin-like domain could
CC       be involved in the binding to egg integrin receptor and thus could
CC       mediate sperm/egg binding. {ECO:0000250}.
CC   -!- PTM: The prodomain and the metalloprotease-like domain are cleaved
CC       during the epididymal maturation of the spermatozoa. {ECO:0000250}.
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DR   EMBL; AJ133004; CAB40812.1; -; mRNA.
DR   EMBL; AY358321; AAQ88687.1; -; mRNA.
DR   EMBL; AK313961; BAG36677.1; -; mRNA.
DR   EMBL; AC109633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034624; AAH34624.1; -; mRNA.
DR   EMBL; BC070279; AAH70279.1; -; mRNA.
DR   EMBL; BC121045; AAI21046.1; -; mRNA.
DR   CCDS; CCDS55225.1; -. [Q9Y3Q7-3]
DR   CCDS; CCDS6113.1; -. [Q9Y3Q7-1]
DR   CCDS; CCDS83287.1; -. [Q9Y3Q7-2]
DR   RefSeq; NP_001177885.1; NM_001190956.1. [Q9Y3Q7-3]
DR   RefSeq; NP_001307242.1; NM_001320313.1. [Q9Y3Q7-2]
DR   RefSeq; NP_055052.1; NM_014237.2. [Q9Y3Q7-1]
DR   AlphaFoldDB; Q9Y3Q7; -.
DR   SMR; Q9Y3Q7; -.
DR   BioGRID; 114285; 29.
DR   STRING; 9606.ENSP00000265707; -.
DR   MEROPS; M12.957; -.
DR   GlyCosmos; Q9Y3Q7; 12 sites, No reported glycans.
DR   GlyGen; Q9Y3Q7; 12 sites.
DR   iPTMnet; Q9Y3Q7; -.
DR   PhosphoSitePlus; Q9Y3Q7; -.
DR   BioMuta; ADAM18; -.
DR   DMDM; 20137582; -.
DR   MassIVE; Q9Y3Q7; -.
DR   PaxDb; 9606-ENSP00000265707; -.
DR   PeptideAtlas; Q9Y3Q7; -.
DR   ProteomicsDB; 86061; -. [Q9Y3Q7-1]
DR   ProteomicsDB; 86062; -. [Q9Y3Q7-2]
DR   Antibodypedia; 23870; 45 antibodies from 8 providers.
DR   DNASU; 8749; -.
DR   Ensembl; ENST00000265707.10; ENSP00000265707.5; ENSG00000168619.16. [Q9Y3Q7-1]
DR   Ensembl; ENST00000379866.5; ENSP00000369195.1; ENSG00000168619.16. [Q9Y3Q7-2]
DR   Ensembl; ENST00000520772.5; ENSP00000429908.1; ENSG00000168619.16. [Q9Y3Q7-3]
DR   Ensembl; ENST00000613609.4; ENSP00000482348.1; ENSG00000278548.4. [Q9Y3Q7-1]
DR   Ensembl; ENST00000633688.1; ENSP00000488128.1; ENSG00000278548.4. [Q9Y3Q7-3]
DR   Ensembl; ENST00000633768.1; ENSP00000488176.1; ENSG00000278548.4. [Q9Y3Q7-2]
DR   GeneID; 8749; -.
DR   KEGG; hsa:8749; -.
DR   MANE-Select; ENST00000265707.10; ENSP00000265707.5; NM_014237.3; NP_055052.1.
DR   UCSC; uc003xnh.4; human. [Q9Y3Q7-1]
DR   AGR; HGNC:196; -.
DR   CTD; 8749; -.
DR   DisGeNET; 8749; -.
DR   GeneCards; ADAM18; -.
DR   HGNC; HGNC:196; ADAM18.
DR   HPA; ENSG00000168619; Tissue enriched (testis).
DR   MIM; 619495; gene.
DR   neXtProt; NX_Q9Y3Q7; -.
DR   OpenTargets; ENSG00000168619; -.
DR   PharmGKB; PA24513; -.
DR   VEuPathDB; HostDB:ENSG00000168619; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000162281; -.
DR   HOGENOM; CLU_012714_4_3_1; -.
DR   InParanoid; Q9Y3Q7; -.
DR   OMA; GPQMYCV; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q9Y3Q7; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q9Y3Q7; -.
DR   BioGRID-ORCS; 8749; 12 hits in 1142 CRISPR screens.
DR   ChiTaRS; ADAM18; human.
DR   GeneWiki; ADAM18; -.
DR   GenomeRNAi; 8749; -.
DR   Pharos; Q9Y3Q7; Tdark.
DR   PRO; PR:Q9Y3Q7; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9Y3Q7; Protein.
DR   Bgee; ENSG00000168619; Expressed in testis and 21 other cell types or tissues.
DR   ExpressionAtlas; Q9Y3Q7; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
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; 3.40.390.10; 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; 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:SF158; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 18; 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   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   Genevisible; Q9Y3Q7; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..184
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000029096"
FT   CHAIN           185..739
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 18"
FT                   /id="PRO_0000029097"
FT   TOPO_DOM        177..687
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..739
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          184..381
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          390..479
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          620..654
FT                   /note="EGF-like"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        611
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        293..376
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        450..471
FT                   /evidence="ECO:0000250"
FT   DISULFID        624..636
FT                   /evidence="ECO:0000250"
FT   DISULFID        630..642
FT                   /evidence="ECO:0000250"
FT   DISULFID        644..653
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         175..182
FT                   /note="IKNLSKLL -> VTVIILML (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043285"
FT   VAR_SEQ         183..739
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043286"
FT   VAR_SEQ         197..220
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_012033"
FT   VARIANT         170
FT                   /note="P -> S (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267601916)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066312"
FT   VARIANT         212
FT                   /note="V -> F (in dbSNP:rs10093794)"
FT                   /id="VAR_051588"
FT   VARIANT         284
FT                   /note="V -> G (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066313"
FT   VARIANT         344
FT                   /note="M -> I (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation; dbSNP:rs267601918)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066314"
FT   VARIANT         362
FT                   /note="M -> K (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066315"
FT   VARIANT         536
FT                   /note="S -> L (in a cutaneous metastatic melanoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21618342"
FT                   /id="VAR_066316"
SQ   SEQUENCE   739 AA;  82856 MW;  2D8BE9A975072CDD CRC64;
     MFLLLALLTE LGRLQAHEGS EGIFLHVTVP RKIKSNDSEV SERKMIYIIT IDGQPYTLHL
     GKQSFLPQNF LVYTYNETGS LHSVSPYFMM HCHYQGYAAE FPNSFVTLSI CSGLRGFLQF
     ENISYGIEPV ESSARFEHII YQMKNNDPNV SILAVNYSHI WQKDQPYKVP LNSQIKNLSK
     LLPQYLEIYI IVEKALYDYM GSEMMAVTQK IVQVIGLVNT MFTQFKLTVI LSSLELWSNE
     NQISTSGDAD DILQRFLAWK RDYLILRPHD IAYLLVYRKH PKYVGATFPG TVCNKSYDAG
     IAMYPDAIGL EGFSVIIAQL LGLNVGLTYD DITQCFCLRA TCIMNHEAVS ASGRKIFSNC
     SMHDYRYFVS KFETKCLQKL SNLQPLHQNQ PVCGNGILES NEECDCGNKN ECQFKKCCDY
     NTCKLKGSVK CGSGPCCTSK CELSIAGTPC RKSIDPECDF TEYCNGTSSN CVPDTYALNG
     RLCKLGTAYC YNGQCQTTDN QCAKIFGKGA QGAPFACFKE VNSLHERSEN CGFKNSQPLP
     CERKDVLCGK LACVQPHKNA NKSDAQSTVY SYIQDHVCVS IATGSSMRSD GTDNAYVADG
     TMCGPEMYCV NKTCRKVHLM GYNCNATTKC KGKGICNNFG NCQCFPGHRP PDCKFQFGSP
     GGSIDDGNFQ KSGDFYTEKG YNTHWNNWFI LSFCIFLPFF IVFTTVIFKR NEISKSCNRE
     NAEYNRNSSV VSESDDVGH
//