PCD12_HUMAN
ID PCD12_HUMAN Reviewed; 1184 AA.
AC Q9NPG4; Q6UXB6; Q96KB8; Q9H7Y6; Q9H8E0;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protocadherin-12 {ECO:0000305};
DE AltName: Full=Vascular cadherin-2 {ECO:0000303|PubMed:11063261};
DE AltName: Full=Vascular endothelial cadherin-2 {ECO:0000303|PubMed:11063261};
DE Short=VE-cad-2 {ECO:0000303|PubMed:11063261};
DE Short=VE-cadherin-2 {ECO:0000303|PubMed:11063261};
DE Contains:
DE RecName: Full=Protocadherin-12, secreted form {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDH12 {ECO:0000312|HGNC:HGNC:8657};
GN ORFNames=UNQ395/PRO731 {ECO:0000303|PubMed:12975309};
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].
RX PubMed=10716726; DOI=10.1073/pnas.97.7.3124;
RA Wu Q., Maniatis T.;
RT "Large exons encoding multiple ectodomains are a characteristic feature of
RT protocadherin genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal kidney;
RX PubMed=11063261; DOI=10.1007/s003350010186;
RA Ludwig D., Lorenz J., Dejana E., Bohlen P., Hicklin D.J., Witte L.,
RA Pytowski B.;
RT "cDNA cloning, chromosomal mapping, and expression analysis of human VE-
RT cadherin-2.";
RL Mamm. Genome 11:1030-1033(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Human vascular cadherin-2.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-385 AND ASN-640.
RC TISSUE=Embryo, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-640.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=21402705; DOI=10.1074/jbc.m111.230045;
RA Bouillot S., Tillet E., Carmona G., Prandini M.H., Gauchez A.S.,
RA Hoffmann P., Alfaidy N., Cand F., Huber P.;
RT "Protocadherin-12 cleavage is a regulated process mediated by ADAM10
RT protein: evidence of shedding up-regulation in pre-eclampsia.";
RL J. Biol. Chem. 286:15195-15204(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN DMJDS1, AND VARIANT DMJDS1 839-ARG--LEU-1184 DEL.
RX PubMed=27164683; DOI=10.1212/wnl.0000000000002704;
RA Aran A., Rosenfeld N., Jaron R., Renbaum P., Zuckerman S., Fridman H.,
RA Zeligson S., Segel R., Kohn Y., Kamal L., Kanaan M., Segev Y., Mazaki E.,
RA Rabinowitz R., Shen O., Lee M., Walsh T., King M.C., Gulsuner S.,
RA Levy-Lahad E.;
RT "Loss of function of PCDH12 underlies recessive microcephaly mimicking
RT intrauterine infection.";
RL Neurology 86:2016-2024(2016).
RN [9]
RP VARIANT GLY-55, AND VARIANTS DMJDS1 ILE-147; ASN-332 AND SER-1091.
RX PubMed=28804758; DOI=10.1212/nxg.0000000000000166;
RA Nicolas G., Sanchez-Contreras M., Ramos E.M., Lemos R.R., Ferreira J.,
RA Moura D., Sobrido M.J., Richard A.C., Lopez A.R., Legati A., Deleuze J.F.,
RA Boland A., Quenez O., Krystkowiak P., Favrole P., Geschwind D.H., Aran A.,
RA Segel R., Levy-Lahad E., Dickson D.W., Coppola G., Rademakers R.,
RA de Oliveira J.R.M.;
RT "variants.";
RL Neurol. Genet. 3:E166-E166(2017).
CC -!- FUNCTION: Cellular adhesion molecule that may play an important role in
CC cell-cell interactions at interendothelial junctions (By similarity).
CC Acts as a regulator of cell migration, probably via increasing cell-
CC cell adhesion (PubMed:21402705). Promotes homotypic calcium-dependent
CC aggregation and adhesion and clusters at intercellular junctions (By
CC similarity). Unable to bind to catenins, weakly associates with the
CC cytoskeleton (By similarity). {ECO:0000250|UniProtKB:O55134,
CC ECO:0000269|PubMed:21402705}.
CC -!- SUBCELLULAR LOCATION: [Protocadherin-12]: Cell membrane
CC {ECO:0000269|PubMed:21402705}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell junction {ECO:0000250|UniProtKB:O55134}.
CC -!- SUBCELLULAR LOCATION: [Protocadherin-12, secreted form]: Secreted
CC {ECO:0000269|PubMed:21402705}. Note=The secreted form is produced
CC following cleavage by ADAM10. {ECO:0000269|PubMed:21402705}.
CC -!- TISSUE SPECIFICITY: Expressed in highly vascularized tissues including
CC the heart and placenta, but most tissues contain a low level of
CC expression (PubMed:11063261). Prominent expression in the spleen
CC (PubMed:11063261). Present in villous and extravillous trophoblast (at
CC protein level) (PubMed:21402705). {ECO:0000269|PubMed:11063261,
CC ECO:0000269|PubMed:21402705}.
CC -!- PTM: [Protocadherin-12]: Cleaved by ADAM10 close to the transmembrane
CC domain to release the Protocadherin-12, secreted form in the serum.
CC Cleavage results in reduced cellular adhesion in a cell migration
CC assay. {ECO:0000269|PubMed:21402705}.
CC -!- DISEASE: Diencephalic-mesencephalic junction dysplasia syndrome 1
CC (DMJDS1) [MIM:251280]: An autosomal recessive syndrome characterized by
CC severe global developmental delay with profound intellectual
CC disability, spasticity or dystonia, and congenital microcephaly. Brain
CC imaging shows hypothalamic midbrain dysplasia, diencephalic-
CC mesencephalic dysplasia, and intracerebral calcifications.
CC {ECO:0000269|PubMed:27164683, ECO:0000269|PubMed:28804758}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF231025; AAF61931.1; -; mRNA.
DR EMBL; AF240635; AAF73962.1; -; mRNA.
DR EMBL; AB026893; BAA95162.1; -; mRNA.
DR EMBL; AK023785; BAB14677.1; -; mRNA.
DR EMBL; AK024140; BAB14837.1; -; mRNA.
DR EMBL; AK027282; BAB55016.1; -; mRNA.
DR EMBL; AY358428; AAQ88794.1; -; mRNA.
DR CCDS; CCDS4269.1; -.
DR RefSeq; NP_057664.1; NM_016580.3.
DR AlphaFoldDB; Q9NPG4; -.
DR SMR; Q9NPG4; -.
DR BioGRID; 119445; 23.
DR DIP; DIP-47292N; -.
DR IntAct; Q9NPG4; 20.
DR MINT; Q9NPG4; -.
DR STRING; 9606.ENSP00000231484; -.
DR GlyGen; Q9NPG4; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPG4; -.
DR PhosphoSitePlus; Q9NPG4; -.
DR BioMuta; PCDH12; -.
DR DMDM; 22095989; -.
DR EPD; Q9NPG4; -.
DR jPOST; Q9NPG4; -.
DR MassIVE; Q9NPG4; -.
DR PaxDb; Q9NPG4; -.
DR PeptideAtlas; Q9NPG4; -.
DR PRIDE; Q9NPG4; -.
DR ProteomicsDB; 81993; -.
DR Antibodypedia; 27396; 89 antibodies from 26 providers.
DR DNASU; 51294; -.
DR Ensembl; ENST00000231484.4; ENSP00000231484.3; ENSG00000113555.6.
DR GeneID; 51294; -.
DR KEGG; hsa:51294; -.
DR MANE-Select; ENST00000231484.4; ENSP00000231484.3; NM_016580.4; NP_057664.1.
DR UCSC; uc003llx.4; human.
DR CTD; 51294; -.
DR DisGeNET; 51294; -.
DR GeneCards; PCDH12; -.
DR HGNC; HGNC:8657; PCDH12.
DR HPA; ENSG00000113555; Tissue enhanced (placenta).
DR MalaCards; PCDH12; -.
DR MIM; 251280; phenotype.
DR MIM; 605622; gene.
DR neXtProt; NX_Q9NPG4; -.
DR OpenTargets; ENSG00000113555; -.
DR Orphanet; 319192; Diencephalic-mesencephalic junction dysplasia.
DR PharmGKB; PA32998; -.
DR VEuPathDB; HostDB:ENSG00000113555; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160403; -.
DR HOGENOM; CLU_006480_1_2_1; -.
DR InParanoid; Q9NPG4; -.
DR OMA; REQWPKY; -.
DR OrthoDB; 64478at2759; -.
DR PhylomeDB; Q9NPG4; -.
DR TreeFam; TF352008; -.
DR PathwayCommons; Q9NPG4; -.
DR SignaLink; Q9NPG4; -.
DR BioGRID-ORCS; 51294; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; PCDH12; human.
DR GeneWiki; PCDH12; -.
DR GenomeRNAi; 51294; -.
DR Pharos; Q9NPG4; Tbio.
DR PRO; PR:Q9NPG4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NPG4; protein.
DR Bgee; ENSG00000113555; Expressed in tendon of biceps brachii and 153 other tissues.
DR ExpressionAtlas; Q9NPG4; baseline and differential.
DR Genevisible; Q9NPG4; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:Ensembl.
DR GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl.
DR GO; GO:0008038; P:neuron recognition; TAS:ProtInc.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030720; Protocadherin-12.
DR PANTHER; PTHR24028:SF42; PTHR24028:SF42; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Disease variant;
KW Epilepsy; Glycoprotein; Intellectual disability; Membrane; Phosphoprotein;
KW Primary microcephaly; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1184
FT /note="Protocadherin-12"
FT /id="PRO_0000003996"
FT CHAIN 25..?
FT /note="Protocadherin-12, secreted form"
FT /evidence="ECO:0000305|PubMed:21402705"
FT /id="PRO_0000444041"
FT TOPO_DOM 25..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..1184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..244
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 245..352
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 355..460
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 461..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 600..711
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 854..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55134"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 55
FT /note="R -> G (in dbSNP:rs200451693)"
FT /evidence="ECO:0000269|PubMed:28804758"
FT /id="VAR_080385"
FT VARIANT 147
FT /note="S -> I (in DMJDS1; unknown pathological
FT significance; dbSNP:rs759794990)"
FT /evidence="ECO:0000269|PubMed:28804758"
FT /id="VAR_080386"
FT VARIANT 332
FT /note="I -> N (in DMJDS1; unknown pathological
FT significance; dbSNP:rs146725009)"
FT /evidence="ECO:0000269|PubMed:28804758"
FT /id="VAR_080387"
FT VARIANT 385
FT /note="H -> N (in dbSNP:rs164075)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_020368"
FT VARIANT 640
FT /note="S -> N (in dbSNP:rs164515)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_020369"
FT VARIANT 839..1184
FT /note="Missing (in DMJDS1)"
FT /evidence="ECO:0000269|PubMed:27164683"
FT /id="VAR_080388"
FT VARIANT 1091
FT /note="G -> S (in DMJDS1; unknown pathological
FT significance; dbSNP:rs779814208)"
FT /evidence="ECO:0000269|PubMed:28804758"
FT /id="VAR_080389"
FT CONFLICT 385..386
FT /note="HN -> KD (in Ref. 4; BAB55016)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="VH -> LG (in Ref. 4; BAB55016)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="A -> V (in Ref. 4; BAB14677)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="R -> W (in Ref. 4; BAB14677)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="A -> T (in Ref. 4; BAB14837)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="H -> Y (in Ref. 4; BAB14837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="S -> C (in Ref. 4; BAB14677)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="S -> SSSS (in Ref. 4; BAB14837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1184 AA; 128995 MW; 45314473DC503E8D CRC64;
MMQLLQLLLG LLGPGGYLFL LGDCQEVTTL TVKYQVSEEV PSGTVIGKLS QELGREERRR
QAGAAFQVLQ LPQALPIQVD SEEGLLSTGR RLDREQLCRQ WDPCLVSFDV LATGDLALIH
VEIQVLDIND HQPRFPKGEQ ELEISESASL RTRIPLDRAL DPDTGPNTLH TYTLSPSEHF
ALDVIVGPDE TKHAELIVVK ELDREIHSFF DLVLTAYDNG NPPKSGTSLV KVNVLDSNDN
SPAFAESSLA LEIQEDAAPG TLLIKLTATD PDQGPNGEVE FFLSKHMPPE VLDTFSIDAK
TGQVILRRPL DYEKNPAYEV DVQARDLGPN PIPAHCKVLI KVLDVNDNIP SIHVTWASQP
SLVSEALPKD SFIALVMADD LDSGHNGLVH CWLSQELGHF RLKRTNGNTY MLLTNATLDR
EQWPKYTLTL LAQDQGLQPL SAKKQLSIQI SDINDNAPVF EKSRYEVSTR ENNLPSLHLI
TIKAHDADLG INGKVSYRIQ DSPVAHLVAI DSNTGEVTAQ RSLNYEEMAG FEFQVIAEDS
GQPMLASSVS VWVSLLDAND NAPEVVQPVL SDGKASLSVL VNASTGHLLV PIETPNGLGP
AGTDTPPLAT HSSRPFLLTT IVARDADSGA NGEPLYSIRS GNEAHLFILN PHTGQLFVNV
TNASSLIGSE WELEIVVEDQ GSPPLQTRAL LRVMFVTSVD HLRDSARKPG ALSMSMLTVI
CLAVLLGIFG LILALFMSIC RTEKKDNRAY NCREAESTYR QQPKRPQKHI QKADIHLVPV
LRGQAGEPCE VGQSHKDVDK EAMMEAGWDP CLQAPFHLTP TLYRTLRNQG NQGAPAESRE
VLQDTVNLLF NHPRQRNASR ENLNLPEPQP ATGQPRSRPL KVAGSPTGRL AGDQGSEEAP
QRPPASSATL RRQRHLNGKV SPEKESGPRQ ILRSLVRLSV AAFAERNPVE ELTVDSPPVQ
QISQLLSLLH QGQFQPKPNH RGNKYLAKPG GSRSAIPDTD GPSARAGGQT DPEQEEGPLD
PEEDLSVKQL LEEELSSLLD PSTGLALDRL SAPDPAWMAR LSLPLTTNYR DNVISPDAAA
TEEPRTFQTF GKAEAPELSP TGTRLASTFV SEMSSLLEML LEQRSSMPVE AASEALRRLS
VCGRTLSLDL ATSAASGMKV QGDPGGKTGT EGKSRGSSSS SRCL
