ADA30_HUMAN
ID ADA30_HUMAN Reviewed; 790 AA.
AC Q9UKF2; A8K8W8; Q5T3X6; Q9UKF1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 30;
DE Short=ADAM 30;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAM30; ORFNames=UNQ2509/PRO5997;
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 ALPHA AND BETA), VARIANT PRO-359, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10512762; DOI=10.1006/bbrc.1999.1322;
RA Cerretti D.P., DuBose R.F., Black R.A., Nelson N.;
RT "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that
RT show testis-specific gene expression.";
RL Biochem. Biophys. Res. Commun. 263:810-815(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
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 ALPHA), AND VARIANT
RP PRO-359.
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=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 [5]
RP FUNCTION, INTERACTION WITH CTSD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF HIS-338; HIS-342 AND HIS-348.
RX PubMed=27333034; DOI=10.1016/j.ebiom.2016.06.002;
RA Letronne F., Laumet G., Ayral A.M., Chapuis J., Demiautte F., Laga M.,
RA Vandenberghe M.E., Malmanche N., Leroux F., Eysert F., Sottejeau Y.,
RA Chami L., Flaig A., Bauer C., Dourlen P., Lesaffre M., Delay C., Huot L.,
RA Dumont J., Werkmeister E., Lafont F., Mendes T., Hansmannel F., Dermaut B.,
RA Deprez B., Herard A.S., Dhenain M., Souedet N., Pasquier F., Tulasne D.,
RA Berr C., Hauw J.J., Lemoine Y., Amouyel P., Mann D., Deprez R., Checler F.,
RA Hot D., Delzescaux T., Gevaert K., Lambert J.C.;
RT "ADAM30 Downregulates APP-Linked Defects Through Cathepsin D Activation in
RT Alzheimer's Disease.";
RL EBioMedicine 9:278-292(2016).
CC -!- FUNCTION: Plays a role in lysosomal amyloid precursor protein (APP)
CC processing by cleaving and activating CTSD/cathepsin D which leads to
CC APP degradation (PubMed:27333034). {ECO:0000269|PubMed:27333034}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with CTSD; this leads to activation of CTSD.
CC {ECO:0000269|PubMed:27333034}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:27333034}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9UKF2-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9UKF2-2; Sequence=VSP_005494;
CC -!- TISSUE SPECIFICITY: Expressed in brain neurons (at protein level)
CC (PubMed:27333034). Expressed in testis (PubMed:10512762).
CC {ECO:0000269|PubMed:10512762, ECO:0000269|PubMed:27333034}.
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.
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DR EMBL; AF171932; AAF03780.1; -; mRNA.
DR EMBL; AF171933; AAF03781.1; -; mRNA.
DR EMBL; AY358734; AAQ89096.1; -; mRNA.
DR EMBL; AK292483; BAF85172.1; -; mRNA.
DR EMBL; AL359752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS907.1; -. [Q9UKF2-1]
DR RefSeq; NP_068566.2; NM_021794.3. [Q9UKF2-1]
DR AlphaFoldDB; Q9UKF2; -.
DR SMR; Q9UKF2; -.
DR BioGRID; 116267; 70.
DR IntAct; Q9UKF2; 14.
DR STRING; 9606.ENSP00000358407; -.
DR MEROPS; M12.232; -.
DR GlyGen; Q9UKF2; 5 sites.
DR iPTMnet; Q9UKF2; -.
DR PhosphoSitePlus; Q9UKF2; -.
DR BioMuta; ADAM30; -.
DR DMDM; 47117918; -.
DR MassIVE; Q9UKF2; -.
DR PaxDb; Q9UKF2; -.
DR PeptideAtlas; Q9UKF2; -.
DR PRIDE; Q9UKF2; -.
DR ProteomicsDB; 84777; -. [Q9UKF2-1]
DR ProteomicsDB; 84778; -. [Q9UKF2-2]
DR Antibodypedia; 20207; 85 antibodies from 21 providers.
DR DNASU; 11085; -.
DR Ensembl; ENST00000369400.2; ENSP00000358407.1; ENSG00000134249.7. [Q9UKF2-1]
DR GeneID; 11085; -.
DR KEGG; hsa:11085; -.
DR MANE-Select; ENST00000369400.2; ENSP00000358407.1; NM_021794.4; NP_068566.2.
DR UCSC; uc001eij.4; human. [Q9UKF2-1]
DR CTD; 11085; -.
DR DisGeNET; 11085; -.
DR GeneCards; ADAM30; -.
DR HGNC; HGNC:208; ADAM30.
DR HPA; ENSG00000134249; Tissue enriched (testis).
DR MIM; 604779; gene.
DR neXtProt; NX_Q9UKF2; -.
DR OpenTargets; ENSG00000134249; -.
DR PharmGKB; PA24525; -.
DR VEuPathDB; HostDB:ENSG00000134249; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162954; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q9UKF2; -.
DR OMA; ICGRLQC; -.
DR PhylomeDB; Q9UKF2; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q9UKF2; -.
DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR SignaLink; Q9UKF2; -.
DR BioGRID-ORCS; 11085; 11 hits in 1071 CRISPR screens.
DR GenomeRNAi; 11085; -.
DR Pharos; Q9UKF2; Tdark.
DR PRO; PR:Q9UKF2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UKF2; protein.
DR Bgee; ENSG00000134249; Expressed in sperm and 19 other tissues.
DR Genevisible; Q9UKF2; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 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 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; SSF57552; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Endosome;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..198
FT /evidence="ECO:0000250"
FT /id="PRO_0000029136"
FT CHAIN 199..790
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 30"
FT /id="PRO_0000029137"
FT TOPO_DOM 199..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 399..485
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 629..663
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 732..740
FT /note="1"
FT REPEAT 741..749
FT /note="2"
FT REPEAT 750..758
FT /note="3"
FT REPEAT 759..767
FT /note="4"
FT REPEAT 768..776
FT /note="5"
FT REGION 720..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..776
FT /note="5 X 9 AA approximate repeats"
FT MOTIF 170..177
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 720..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 172
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 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
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 313..388
FT /evidence="ECO:0000250"
FT DISULFID 353..373
FT /evidence="ECO:0000250"
FT DISULFID 355..361
FT /evidence="ECO:0000250"
FT DISULFID 457..477
FT /evidence="ECO:0000250"
FT DISULFID 633..644
FT /evidence="ECO:0000250"
FT DISULFID 638..650
FT /evidence="ECO:0000250"
FT DISULFID 652..661
FT /evidence="ECO:0000250"
FT VAR_SEQ 763..771
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10512762"
FT /id="VSP_005494"
FT VARIANT 359
FT /note="L -> P (in dbSNP:rs2641348)"
FT /evidence="ECO:0000269|PubMed:10512762,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_024597"
FT VARIANT 737
FT /note="T -> A (in dbSNP:rs35273427)"
FT /id="VAR_061738"
FT MUTAGEN 338
FT /note="H->L: Loss of enzymatic activity; when associated
FT with L-342 and L-348."
FT /evidence="ECO:0000269|PubMed:27333034"
FT MUTAGEN 342
FT /note="H->L: Loss of enzymatic activity; when associated
FT with L-338 and L-348."
FT /evidence="ECO:0000269|PubMed:27333034"
FT MUTAGEN 348
FT /note="H->L: Loss of enzymatic activity; when associated
FT with L-338 and L-342."
FT /evidence="ECO:0000269|PubMed:27333034"
FT CONFLICT 336
FT /note="S -> P (in Ref. 1; AAF03781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 88940 MW; 42EC8A5F6B5ACDA3 CRC64;
MRSVQIFLSQ CRLLLLLVPT MLLKSLGEDV IFHPEGEFDS YEVTIPEKLS FRGEVQGVVS
PVSYLLQLKG KKHVLHLWPK RLLLPRHLRV FSFTEHGELL EDHPYIPKDC NYMGSVKESL
DSKATISTCM GGLRGVFNID AKHYQIEPLK ASPSFEHVVY LLKKEQFGNQ VCGLSDDEIE
WQMAPYENKA RLRDFPGSYK HPKYLELILL FDQSRYRFVN NNLSQVIHDA ILLTGIMDTY
FQDVRMRIHL KALEVWTDFN KIRVGYPELA EVLGRFVIYK KSVLNARLSS DWAHLYLQRK
YNDALAWSFG KVCSLEYAGS VSTLLDTNIL APATWSAHEL GHAVGMSHDE QYCQCRGRLN
CIMGSGRTGF SNCSYISFFK HISSGATCLN NIPGLGYVLK RCGNKIVEDN EECDCGSTEE
CQKDRCCQSN CKLQPGANCS IGLCCHDCRF RPSGYVCRQE GNECDLAEYC DGNSSSCPND
VYKQDGTPCK YEGRCFRKGC RSRYMQCQSI FGPDAMEAPS ECYDAVNLIG DQFGNCEITG
IRNFKKCESA NSICGRLQCI NVETIPDLPE HTTIISTHLQ AENLMCWGTG YHLSMKPMGI
PDLGMINDGT SCGEGRVCFK KNCVNSSVLQ FDCLPEKCNT RGVCNNRKNC HCMYGWAPPF
CEEVGYGGSI DSGPPGLLRG AIPSSIWVVS IIMFRLILLI LSVVFVFFRQ VIGNHLKPKQ
EKMPLSKAKT EQEESKTKTV QEESKTKTGQ EESEAKTGQE ESKAKTGQEE SKANIESKRP
KAKSVKKQKK
