CPMD8_HUMAN
ID CPMD8_HUMAN Reviewed; 1885 AA.
AC Q8IZJ3; Q8NC09; Q9ULD7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 8 {ECO:0000303|PubMed:15177561};
DE Flags: Precursor;
GN Name=CPAMD8 {ECO:0000312|HGNC:HGNC:23228};
GN Synonyms=KIAA1283 {ECO:0000312|EMBL:BAA86597.1};
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), IDENTIFICATION BY MASS
RP SPECTROMETRY, TISSUE SPECIFICITY, CLEAVAGE BY FURIN-LIKE PROTEASE,
RP SUBCELLULAR LOCATION, INDUCTION BY IL1B AND IL6, INTERACTION WITH HEPARIN,
RP AND VARIANTS GLN-294 AND ILE-1268.
RX PubMed=15177561; DOI=10.1016/j.ygeno.2003.12.005;
RA Li Z.-F., Wu X.-H., Engvall E.;
RT "Identification and characterization of CPAMD8, a novel member of the
RT complement 3/alpha2-macroglobulin family with a C-terminal Kazal domain.";
RL Genomics 83:1083-1093(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1885 (ISOFORM 1), AND VARIANTS
RP GLN-294 AND ILE-1268.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1479-1885 (ISOFORM 2).
RC TISSUE=Placenta;
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 [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INVOLVEMENT IN ASGD8, AND VARIANT
RP ASGD8 PRO-1404.
RX PubMed=27839872; DOI=10.1016/j.ajhg.2016.09.022;
RA Cheong S.S., Hentschel L., Davidson A.E., Gerrelli D., Davie R., Rizzo R.,
RA Pontikos N., Plagnol V., Moore A.T., Sowden J.C., Michaelides M., Snead M.,
RA Tuft S.J., Hardcastle A.J.;
RT "Mutations in CPAMD8 cause a unique form of autosomal-recessive anterior
RT segment dysgenesis.";
RL Am. J. Hum. Genet. 99:1338-1352(2016).
CC -!- SUBUNIT: Interacts with heparin. {ECO:0000269|PubMed:15177561}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15177561}. Cell
CC membrane {ECO:0000269|PubMed:15177561}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15177561}; Extracellular side
CC {ECO:0000269|PubMed:15177561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZJ3-2; Sequence=VSP_031137, VSP_031138;
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney, brain and testis
CC and to a lower extent in heart, liver and small intestine
CC (PubMed:15177561). Expressed in the lens, cornea and retina. Strongly
CC expressed in the distal tips of the retinal neuroepithelium that form
CC the iris and ciliary body (PubMed:27839872).
CC {ECO:0000269|PubMed:15177561, ECO:0000269|PubMed:27839872}.
CC -!- DEVELOPMENTAL STAGE: Expressed early in development of the eye (week 9
CC to week 22 of gestation). {ECO:0000269|PubMed:27839872}.
CC -!- INDUCTION: Up-regulated by IL1B/interleukin-1 beta and IL6/interleukin-
CC 6. {ECO:0000269|PubMed:15177561}.
CC -!- PTM: Proteolytically cleaved into 2 chains of about 70 and 130 kDa. The
CC fragments are not connected by disulfide bonds.
CC {ECO:0000269|PubMed:15177561}.
CC -!- DISEASE: Anterior segment dysgenesis 8 (ASGD8) [MIM:617319]: A form of
CC anterior segment dysgenesis, a group of defects affecting anterior
CC structures of the eye including cornea, iris, lens, trabecular
CC meshwork, and Schlemm canal. Anterior segment dysgeneses result from
CC abnormal migration or differentiation of the neural crest derived
CC mesenchymal cells that give rise to components of the anterior chamber
CC during eye development. Different anterior segment anomalies may exist
CC alone or in combination, including iris hypoplasia, enlarged or reduced
CC corneal diameter, corneal vascularization and opacity, posterior
CC embryotoxon, corectopia, polycoria, abnormal iridocorneal angle,
CC ectopia lentis, and anterior synechiae between the iris and posterior
CC corneal surface. Clinical conditions falling within the phenotypic
CC spectrum of anterior segment dysgeneses include aniridia, Axenfeld
CC anomaly, Reiger anomaly/syndrome, Peters anomaly, and
CC iridogoniodysgenesis. ASGD8 patients predominantly manifest iris and
CC lens abnormalities, in the absence of retinal abnormalities or extra-
CC ocular features. ASGD8 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:27839872}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11400.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY101765; AAM50084.1; -; mRNA.
DR EMBL; AC008737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033109; BAA86597.1; -; mRNA.
DR EMBL; AK075099; BAC11400.1; ALT_INIT; mRNA.
DR CCDS; CCDS42519.1; -. [Q8IZJ3-1]
DR AlphaFoldDB; Q8IZJ3; -.
DR SMR; Q8IZJ3; -.
DR BioGRID; 118033; 6.
DR IntAct; Q8IZJ3; 3.
DR STRING; 9606.ENSP00000402505; -.
DR GlyGen; Q8IZJ3; 6 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZJ3; -.
DR PhosphoSitePlus; Q8IZJ3; -.
DR SwissPalm; Q8IZJ3; -.
DR BioMuta; CPAMD8; -.
DR DMDM; 259016204; -.
DR EPD; Q8IZJ3; -.
DR jPOST; Q8IZJ3; -.
DR MassIVE; Q8IZJ3; -.
DR PaxDb; Q8IZJ3; -.
DR PeptideAtlas; Q8IZJ3; -.
DR PRIDE; Q8IZJ3; -.
DR ProteomicsDB; 71357; -. [Q8IZJ3-1]
DR ProteomicsDB; 71358; -. [Q8IZJ3-2]
DR Antibodypedia; 27470; 28 antibodies from 11 providers.
DR Ensembl; ENST00000443236.7; ENSP00000402505.3; ENSG00000160111.15. [Q8IZJ3-1]
DR Ensembl; ENST00000651564.2; ENSP00000498697.2; ENSG00000160111.15. [Q8IZJ3-2]
DR MANE-Select; ENST00000443236.7; ENSP00000402505.3; NM_015692.5; NP_056507.3.
DR UCSC; uc002nfb.4; human. [Q8IZJ3-1]
DR GeneCards; CPAMD8; -.
DR HGNC; HGNC:23228; CPAMD8.
DR HPA; ENSG00000160111; Tissue enhanced (brain, prostate, seminal vesicle).
DR MalaCards; CPAMD8; -.
DR MIM; 608841; gene.
DR MIM; 617319; phenotype.
DR neXtProt; NX_Q8IZJ3; -.
DR OpenTargets; ENSG00000160111; -.
DR Orphanet; 519388; Autosomal recessive anterior segment dysgenesis.
DR PharmGKB; PA134915057; -.
DR VEuPathDB; HostDB:ENSG00000160111; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000162399; -.
DR HOGENOM; CLU_001634_1_0_1; -.
DR InParanoid; Q8IZJ3; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; Q8IZJ3; -.
DR TreeFam; TF313285; -.
DR PathwayCommons; Q8IZJ3; -.
DR SignaLink; Q8IZJ3; -.
DR BioGRID-ORCS; 27151; 124 hits in 1066 CRISPR screens.
DR ChiTaRS; CPAMD8; human.
DR GenomeRNAi; 27151; -.
DR Pharos; Q8IZJ3; Tbio.
DR PRO; PR:Q8IZJ3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IZJ3; protein.
DR Bgee; ENSG00000160111; Expressed in apex of heart and 156 other tissues.
DR ExpressionAtlas; Q8IZJ3; baseline and differential.
DR Genevisible; Q8IZJ3; HS.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR022041; Methyltransf_FA.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF12248; Methyltransf_FA; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Membrane; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1885
FT /note="C3 and PZP-like alpha-2-macroglobulin domain-
FT containing protein 8"
FT /id="PRO_0000317695"
FT DOMAIN 1706..1757
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1514..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 671..672
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000305"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1712..1742
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 1716..1735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 1724..1755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1809..1815
FT /note="RVTAGPR -> SQSGFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031137"
FT VAR_SEQ 1816..1885
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031138"
FT VARIANT 251
FT /note="R -> W (in dbSNP:rs10426545)"
FT /id="VAR_038655"
FT VARIANT 265
FT /note="M -> T (in dbSNP:rs4808551)"
FT /id="VAR_038656"
FT VARIANT 294
FT /note="R -> Q (in dbSNP:rs3745340)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15177561"
FT /id="VAR_038657"
FT VARIANT 539
FT /note="D -> E (in dbSNP:rs3745335)"
FT /id="VAR_038658"
FT VARIANT 546
FT /note="H -> R (in dbSNP:rs1824152)"
FT /id="VAR_038659"
FT VARIANT 736
FT /note="P -> H (in dbSNP:rs9305083)"
FT /id="VAR_038660"
FT VARIANT 1156
FT /note="V -> I (in dbSNP:rs2250918)"
FT /id="VAR_038661"
FT VARIANT 1268
FT /note="T -> I (in dbSNP:rs706761)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15177561"
FT /id="VAR_038662"
FT VARIANT 1404
FT /note="S -> P (in ASGD8; dbSNP:rs1057519340)"
FT /evidence="ECO:0000269|PubMed:27839872"
FT /id="VAR_077933"
FT VARIANT 1843
FT /note="Q -> R (in dbSNP:rs1054533)"
FT /id="VAR_038663"
FT CONFLICT 1588
FT /note="S -> G (in Ref. 4; BAC11400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1885 AA; 206702 MW; 5AA522DE6155C288 CRC64;
MSGALLWPLL PLLLLLLSAR DGVRAAQPQA PGYLIAAPSV FRAGVEEVIS VTIFNSPREV
TVQAQLVAQG EPVVQSQGAI LDKGTIKLKV PTGLRGQALL KVWGRGWQAE EGPLFHNQTS
VTVDGRGASV FIQTDKPVYR PQHRVLISIF TVSPNLRPVN EKLEAYILDP RGSRMIEWRH
LKPFCCGITN MSFPLSDQPV LGEWFIFVEM QGHAYNKSFE VQKYVLPKFE LLIDPPRYIQ
DLDACETGTV RARYTFGKPV AGALMINMTV NGVGYYSHEV GRPVLRTTKI LGSRDFDICV
RDMIPADVPE HFRGRVSIWA MVTSVDGSQQ VAFDDSTPVQ RQLVDIRYSK DTRKQFKPGL
AYVGKVELSY PDGSPAEGVT VQIKAELTPK DNIYTSEVVS QRGLVGFEIP SIPTSAQHVW
LETKVMALNG KPVGAQYLPS YLSLGSWYSP SQCYLQLQPP SHPLQVGEEA YFSVKSTCPC
NFTLYYEVAA RGNIVLSGQQ PAHTTQQRSK RAAPALEKPI RLTHLSETEP PPAPEAEVDV
CVTSLHLAVT PSMVPLGRLL VFYVRENGEG VADSLQFAVE TFFENQVSVT YSANETQPGE
VVDLRIRAAR GSCVCVAAVD KSVYLLRSGF RLTPAQVFQE LEDYDVSDSF GVSREDGPFW
WAGLTAQRRR RSSVFPWPWG ITKDSGFAFT ETGLVVMTDR VSLNHRQDGG LYTDEAVPAF
QPHTGSLVAV APSRHPPRTE KRKRTFFPET WIWHCLNISD PSGEGTLSVK VPDSITSWVG
EAVALSTSQG LGIAEPSLLK TFKPFFVDFM LPALIIRGEQ VKIPLSVYNY MGTCAEVYMK
LSVPKGIQFV GHPGKRHVTK KMCVAPGEAE PIWVVLSFSD LGLNNITAKA LAYGDTNCCR
DGRSSKHPEE NHADRRVPIG VDHVRRSVMV EAEGVPRAYT YSAFFCPSER VHISTPNKYE
FQYVQRPLRL TRFDVAVRAH NDARVALSSG PQDTAGMIEI VLGGHQNTRS WISTSKMGEP
VASAHTAKIL SWDEFRTFWI SWRGGLIQVG HGPEPSNESV IVAWTLPRPP EVQFIGFSTG
WGSMGEFRIW RKMEVDESYS EAFTLGVPHG AIPGSERATA SIIGDVMGPT LNHLNNLLRL
PFGCGEQNMI HFAPNVFVLK YLQKTQQLSP EVERETTDYL VQGYQRQLTY KRQDGSYSAF
GERDASGSMW LTAFVLKSFA QARSFIFVDP RELAAAKSWI IQQQQADGSF LAVGRVLNKD
IQGGIHGTVP LTAYVVVALL ETGTASEEER GSTDKARHFL ESAAPLAMDP YSCALTTYAL
TLLRSPAAPE ALRKLRSLAI MRDGVTHWSL SNSWDVDKGT FLSFSDRVSQ SVVSAEVEMT
AYALLTYTLL GDVAAALPVV KWLSQQRNAL GGFSSTQDTC VALQALAEYA ILSYAGGINL
TVSLASTNLD YQETFELHRT NQKVLQTAAI PSLPTGLFVS AKGDGCCLMQ IDVTYNVPDP
VAKPAFQLLV SLQEPEAQGR PPPMPASAAE GSRGDWPPAD DDDPAADQHH QEYKVMLEVC
TRWLHAGSSN MAVLEVPLLS GFRADIESLE QLLLDKHMGM KRYEVAGRRV LFYFDEIPSR
CLTCVRFRAL RECVVGRTSA LPVSVYDYYE PAFEATRFYN VSTHSPLARE LCAGPACNEV
ERAPARGPGW FPGESGPAVA PEEGAAIARC GCDHDCGAQG NPVCGSDGVV YASACRLREA
ACRQAAPLEP APPSCCALEQ RLPASSSSTY GDDLASVAPG PLQQDVKLNG AGLEVEDSDP
EPEGEAEDRV TAGPRPPVSS GNLESSTQSA SPFHRWGQTP APQRHSGRVV GAHRPGLLSP
VFVYSPAFQS GGEEGLWMSN TCTLR
