ATS14_HUMAN
ID ATS14_HUMAN Reviewed; 1223 AA.
AC Q8WXS8; Q5T4G0; Q5T4G1; Q8TE55; Q8TEY8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14;
DE Short=ADAM-TS 14;
DE Short=ADAM-TS14;
DE Short=ADAMTS-14;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADAMTS14;
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 A), TISSUE SPECIFICITY, AND VARIANT
RP PRO-590.
RX PubMed=11779638; DOI=10.1016/s0167-4781(01)00329-3;
RA Bolz H., Ramirez A., von Brederlow B., Kubisch C.;
RT "Characterization of ADAMTS14, a novel member of the ADAMTS
RT metalloproteinase family.";
RL Biochim. Biophys. Acta 1522:221-225(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND VARIANT
RP PRO-590.
RC TISSUE=Fetal lung;
RX PubMed=11867212; DOI=10.1016/s0378-1119(01)00861-7;
RA Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.;
RT "Cloning, expression analysis, and structural characterization of seven
RT novel human ADAMTSs, a family of metalloproteinases with disintegrin and
RT thrombospondin-1 domains.";
RL Gene 283:49-62(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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 [MRNA] OF 29-1223 (ISOFORMS B; C AND D), FUNCTION,
RP ALTERNATIVE PROMOTER USAGE, AND VARIANT PRO-590.
RX PubMed=11741898; DOI=10.1074/jbc.m105601200;
RA Colige A., Vandenberghe I., Thiry M., Lambert C.A., Van Beeumen J.,
RA Li S.-W., Prockop D.J., Lapiere C.M., Nusgens B.V.;
RT "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high
RT homology with ADAMTS-2 and ADAMTS-3.";
RL J. Biol. Chem. 277:5756-5766(2002).
RN [6]
RP FUNCTION.
RX PubMed=31152061; DOI=10.1074/jbc.ra119.007806;
RA Rosell-Garcia T., Paradela A., Bravo G., Dupont L., Bekhouche M.,
RA Colige A., Rodriguez-Pascual F.;
RT "Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and
RT ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain.";
RL J. Biol. Chem. 294:11087-11100(2019).
CC -!- FUNCTION: Has aminoprocollagen type I processing activity in the
CC absence of ADAMTS2 (PubMed:11741898). Seems to be synthesized as a
CC latent enzyme that requires activation to display aminoprocollagen
CC peptidase activity (PubMed:11741898). Cleaves lysyl oxidase LOX at a
CC site downstream of its propeptide cleavage site to produce a short LOX
CC form (PubMed:31152061). {ECO:0000269|PubMed:11741898,
CC ECO:0000269|PubMed:31152061}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q8WXS8-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q8WXS8-2; Sequence=VSP_006958;
CC Name=C;
CC IsoId=Q8WXS8-3; Sequence=VSP_006958, VSP_005501;
CC Name=D;
CC IsoId=Q8WXS8-4; Sequence=VSP_005501;
CC -!- TISSUE SPECIFICITY: Expressed in retina and at low levels in brain,
CC lung and placenta (PubMed:11779638). High expression in fetal tissues
CC (PubMed:11867212). {ECO:0000269|PubMed:11779638,
CC ECO:0000269|PubMed:11867212}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix. {ECO:0000250}.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform A]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform B]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform C]: Produced by alternative splicing of isoform
CC B. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform D]: Produced by alternative splicing of isoform
CC A. {ECO:0000305}.
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DR EMBL; AF358666; AAL40229.1; -; mRNA.
DR EMBL; AJ345098; CAC87943.1; -; mRNA.
DR EMBL; AL355344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54409.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54410.1; -; Genomic_DNA.
DR EMBL; AF366351; AAL79814.1; -; mRNA.
DR CCDS; CCDS7306.1; -. [Q8WXS8-1]
DR CCDS; CCDS7307.1; -. [Q8WXS8-4]
DR RefSeq; NP_542453.2; NM_080722.4. [Q8WXS8-1]
DR RefSeq; NP_631894.2; NM_139155.3. [Q8WXS8-4]
DR AlphaFoldDB; Q8WXS8; -.
DR SMR; Q8WXS8; -.
DR BioGRID; 126697; 7.
DR IntAct; Q8WXS8; 1.
DR STRING; 9606.ENSP00000362304; -.
DR MEROPS; M12.024; -.
DR GlyGen; Q8WXS8; 4 sites.
DR iPTMnet; Q8WXS8; -.
DR PhosphoSitePlus; Q8WXS8; -.
DR BioMuta; ADAMTS14; -.
DR DMDM; 317373325; -.
DR MassIVE; Q8WXS8; -.
DR PaxDb; Q8WXS8; -.
DR PeptideAtlas; Q8WXS8; -.
DR PRIDE; Q8WXS8; -.
DR ProteomicsDB; 75096; -. [Q8WXS8-1]
DR ProteomicsDB; 75097; -. [Q8WXS8-2]
DR ProteomicsDB; 75098; -. [Q8WXS8-3]
DR ProteomicsDB; 75099; -. [Q8WXS8-4]
DR Antibodypedia; 29052; 42 antibodies from 16 providers.
DR DNASU; 140766; -.
DR Ensembl; ENST00000373207.2; ENSP00000362303.1; ENSG00000138316.11. [Q8WXS8-1]
DR Ensembl; ENST00000373208.5; ENSP00000362304.1; ENSG00000138316.11. [Q8WXS8-4]
DR GeneID; 140766; -.
DR KEGG; hsa:140766; -.
DR MANE-Select; ENST00000373207.2; ENSP00000362303.1; NM_080722.4; NP_542453.2.
DR UCSC; uc001jrg.4; human. [Q8WXS8-1]
DR CTD; 140766; -.
DR DisGeNET; 140766; -.
DR GeneCards; ADAMTS14; -.
DR HGNC; HGNC:14899; ADAMTS14.
DR HPA; ENSG00000138316; Tissue enhanced (brain, gallbladder, placenta).
DR MIM; 607506; gene.
DR neXtProt; NX_Q8WXS8; -.
DR OpenTargets; ENSG00000138316; -.
DR PharmGKB; PA24540; -.
DR VEuPathDB; HostDB:ENSG00000138316; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158426; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; Q8WXS8; -.
DR OMA; LVPLHGC; -.
DR OrthoDB; 79609at2759; -.
DR PhylomeDB; Q8WXS8; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.14; 2681.
DR PathwayCommons; Q8WXS8; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q8WXS8; -.
DR BioGRID-ORCS; 140766; 6 hits in 1077 CRISPR screens.
DR ChiTaRS; ADAMTS14; human.
DR GenomeRNAi; 140766; -.
DR Pharos; Q8WXS8; Tbio.
DR PRO; PR:Q8WXS8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WXS8; protein.
DR Bgee; ENSG00000138316; Expressed in gall bladder and 126 other tissues.
DR Genevisible; Q8WXS8; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 4.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF82895; SSF82895; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Alternative splicing;
KW Cleavage on pair of basic residues; Collagen degradation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..252
FT /evidence="ECO:0000250"
FT /id="PRO_0000029190"
FT CHAIN 253..1223
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 14"
FT /id="PRO_0000029191"
FT DOMAIN 259..460
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 461..551
FT /note="Disintegrin"
FT DOMAIN 552..607
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 847..907
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 908..967
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 968..1022
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1059..1097
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 730..846
FT /note="Spacer"
FT REGION 1100..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..382
FT /evidence="ECO:0000250"
FT DISULFID 376..455
FT /evidence="ECO:0000250"
FT DISULFID 415..441
FT /evidence="ECO:0000250"
FT DISULFID 482..507
FT /evidence="ECO:0000250"
FT DISULFID 493..516
FT /evidence="ECO:0000250"
FT DISULFID 502..535
FT /evidence="ECO:0000250"
FT DISULFID 529..540
FT /evidence="ECO:0000250"
FT DISULFID 564..601
FT /evidence="ECO:0000250"
FT DISULFID 568..606
FT /evidence="ECO:0000250"
FT DISULFID 579..591
FT /evidence="ECO:0000250"
FT DISULFID 980..1016
FT /evidence="ECO:0000250"
FT DISULFID 984..1021
FT /evidence="ECO:0000250"
FT DISULFID 995..1005
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:11741898"
FT /id="VSP_006958"
FT VAR_SEQ 368
FT /note="G -> GMQG (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:11741898"
FT /id="VSP_005501"
FT VARIANT 179
FT /note="R -> C (in dbSNP:rs34022601)"
FT /id="VAR_047837"
FT VARIANT 590
FT /note="L -> P (in dbSNP:rs10823607)"
FT /evidence="ECO:0000269|PubMed:11741898,
FT ECO:0000269|PubMed:11779638, ECO:0000269|PubMed:11867212"
FT /id="VAR_047838"
FT VARIANT 937
FT /note="L -> M (in dbSNP:rs12774070)"
FT /id="VAR_047839"
FT VARIANT 1017
FT /note="S -> N (in dbSNP:rs10999516)"
FT /id="VAR_047840"
FT VARIANT 1049
FT /note="E -> G (in dbSNP:rs4747096)"
FT /id="VAR_047841"
FT CONFLICT 868
FT /note="Q -> R (in Ref. 2; CAC87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="Q -> H (in Ref. 2; CAC87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="C -> S (in Ref. 2; CAC87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="C -> Y (in Ref. 2; CAC87943)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="N -> S (in Ref. 2; CAC87943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1223 AA; 133888 MW; EEF3229519B3170A CRC64;
MAPLRALLSY LLPLHCALCA AAGSRTPELH LSGKLSDYGV TVPCSTDFRG RFLSHVVSGP
AAASAGSMVV DTPPTLPRHS SHLRVARSPL HPGGTLWPGR VGRHSLYFNV TVFGKELHLR
LRPNRRLVVP GSSVEWQEDF RELFRQPLRQ ECVYTGGVTG MPGAAVAISN CDGLAGLIRT
DSTDFFIEPL ERGQQEKEAS GRTHVVYRRE AVQQEWAEPD GDLHNEAFGL GDLPNLLGLV
GDQLGDTERK RRHAKPGSYS IEVLLVVDDS VVRFHGKEHV QNYVLTLMNI VDEIYHDESL
GVHINIALVR LIMVGYRQSL SLIERGNPSR SLEQVCRWAH SQQRQDPSHA EHHDHVVFLT
RQDFGPSGYA PVTGMCHPLR SCALNHEDGF SSAFVIAHET GHVLGMEHDG QGNGCADETS
LGSVMAPLVQ AAFHRFHWSR CSKLELSRYL PSYDCLLDDP FDPAWPQPPE LPGINYSMDE
QCRFDFGSGY QTCLAFRTFE PCKQLWCSHP DNPYFCKTKK GPPLDGTECA PGKWCFKGHC
IWKSPEQTYG QDGGWSSWTK FGSCSRSCGG GVRSRSRSCN NPSPAYGGRL CLGPMFEYQV
CNSEECPGTY EDFRAQQCAK RNSYYVHQNA KHSWVPYEPD DDAQKCELIC QSADTGDVVF
MNQVVHDGTR CSYRDPYSVC ARGECVPVGC DKEVGSMKAD DKCGVCGGDN SHCRTVKGTL
GKASKQAGAL KLVQIPAGAR HIQIEALEKS PHRIVVKNQV TGSFILNPKG KEATSRTFTA
MGLEWEDAVE DAKESLKTSG PLPEAIAILA LPPTEGGPRS SLAYKYVIHE DLLPLIGSNN
VLLEEMDTYE WALKSWAPCS KACGGGIQFT KYGCRRRRDH HMVQRHLCDH KKRPKPIRRR
CNQHPCSQPV WVTEEWGACS RSCGKLGVQT RGIQCLLPLS NGTHKVMPAK ACAGDRPEAR
RPCLRVPCPA QWRLGAWSQC SATCGEGIQQ RQVVCRTNAN SLGHCEGDRP DTVQVCSLPA
CGGNHQNSTV RADVWELGTP EGQWVPQSEP LHPINKISST EPCTGDRSVF CQMEVLDRYC
SIPGYHRLCC VSCIKKASGP NPGPDPGPTS LPPFSTPGSP LPGPQDPADA AEPPGKPTGS
EDHQHGRATQ LPGALDTSSP GTQHPFAPET PIPGASWSIS PTTPGGLPWG WTQTPTPVPE
DKGQPGEDLR HPGTSLPAAS PVT
