PCDH8_HUMAN
ID PCDH8_HUMAN Reviewed; 1070 AA.
AC O95206; B4DMV7; Q5TAN1; Q5TAN2; Q8IYE9; Q96SF1;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protocadherin-8;
DE AltName: Full=Arcadlin;
DE Flags: Precursor;
GN Name=PCDH8;
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).
RX PubMed=9787079; DOI=10.1006/geno.1998.5467;
RA Strehl S., Glatt K., Liu Q.M., Glatt H., Lalande M.;
RT "Characterization of two novel protocadherins (PCDH8 and PCDH9) localized
RT on human chromosome 13 and mouse chromosome 14.";
RL Genomics 53:81-89(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
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 [7]
RP VARIANTS ARG-7; ALA-39 AND ALA-743.
RX PubMed=12884975; DOI=10.1034/j.1601-183x.2002.10307.x;
RA Bray N.J., Kirov G., Owen R.J., Jacobsen N.J., Georgieva L., Williams H.J.,
RA Norton N., Spurlock G., Jones S., Zammit S., O'Donovan M.C., Owen M.J.;
RT "Screening the human protocadherin 8 (PCDH8) gene in schizophrenia.";
RL Genes Brain Behav. 1:187-191(2002).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-956.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May
CC play a role in activity-induced synaptic reorganization underlying long
CC term memory (By similarity). Could be involved in CDH2 internalization
CC through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role
CC in the down-regulation of dendritic spines, maybe through its action on
CC CDH2 endocytosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The N-terminal extracellular domain forms homophilic
CC interactions; these interactions activate p38 MAPK via TAOK2 and
CC trigger endocytosis. Interacts with CDH2; this interaction may lead to
CC CDH2 cointernalization. Interacts with CDH11. Interacts with TAOK2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Presynaptic cell membrane. Postsynaptic cell membrane.
CC Note=Also expressed in neuronal cell bodies. Localized to excitatory,
CC but not with inhibitory, synapses. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95206-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95206-2; Sequence=VSP_008706;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG60019.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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; AF061573; AAC70009.2; -; mRNA.
DR EMBL; AY013873; AAK21986.1; -; mRNA.
DR EMBL; AL139085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471124; EAW52049.1; -; Genomic_DNA.
DR EMBL; CH471124; EAW52050.1; -; Genomic_DNA.
DR EMBL; BC036025; AAH36025.1; -; mRNA.
DR EMBL; AK297652; BAG60019.1; ALT_SEQ; mRNA.
DR CCDS; CCDS9438.1; -. [O95206-1]
DR CCDS; CCDS9439.1; -. [O95206-2]
DR RefSeq; NP_002581.2; NM_002590.3. [O95206-1]
DR RefSeq; NP_116567.1; NM_032949.2. [O95206-2]
DR PDB; 6VFV; X-ray; 2.90 A; A=490-712.
DR PDBsum; 6VFV; -.
DR AlphaFoldDB; O95206; -.
DR SMR; O95206; -.
DR BioGRID; 111133; 3.
DR IntAct; O95206; 3.
DR MINT; O95206; -.
DR STRING; 9606.ENSP00000367177; -.
DR GlyGen; O95206; 3 sites.
DR iPTMnet; O95206; -.
DR PhosphoSitePlus; O95206; -.
DR BioMuta; PCDH8; -.
DR MassIVE; O95206; -.
DR PaxDb; O95206; -.
DR PeptideAtlas; O95206; -.
DR PRIDE; O95206; -.
DR ProteomicsDB; 50714; -. [O95206-1]
DR ProteomicsDB; 50715; -. [O95206-2]
DR Antibodypedia; 24243; 138 antibodies from 22 providers.
DR DNASU; 5100; -.
DR Ensembl; ENST00000338862.5; ENSP00000341350.4; ENSG00000136099.13. [O95206-2]
DR Ensembl; ENST00000377942.7; ENSP00000367177.3; ENSG00000136099.13. [O95206-1]
DR GeneID; 5100; -.
DR KEGG; hsa:5100; -.
DR MANE-Select; ENST00000377942.7; ENSP00000367177.3; NM_002590.4; NP_002581.2.
DR UCSC; uc001vhi.4; human. [O95206-1]
DR CTD; 5100; -.
DR DisGeNET; 5100; -.
DR GeneCards; PCDH8; -.
DR HGNC; HGNC:8660; PCDH8.
DR HPA; ENSG00000136099; Tissue enriched (brain).
DR MIM; 603580; gene.
DR neXtProt; NX_O95206; -.
DR OpenTargets; ENSG00000136099; -.
DR PharmGKB; PA33007; -.
DR VEuPathDB; HostDB:ENSG00000136099; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155219; -.
DR HOGENOM; CLU_006480_1_2_1; -.
DR InParanoid; O95206; -.
DR OMA; GESSCHF; -.
DR OrthoDB; 64478at2759; -.
DR PhylomeDB; O95206; -.
DR TreeFam; TF352008; -.
DR PathwayCommons; O95206; -.
DR SignaLink; O95206; -.
DR BioGRID-ORCS; 5100; 9 hits in 1057 CRISPR screens.
DR GeneWiki; PCDH8; -.
DR GenomeRNAi; 5100; -.
DR Pharos; O95206; Tbio.
DR PRO; PR:O95206; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O95206; protein.
DR Bgee; ENSG00000136099; Expressed in Brodmann (1909) area 23 and 110 other tissues.
DR ExpressionAtlas; O95206; baseline and differential.
DR Genevisible; O95206; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030711; Protocadherin-8.
DR PANTHER; PTHR24028:SF46; PTHR24028:SF46; 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; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1070
FT /note="Protocadherin-8"
FT /id="PRO_0000003993"
FT TOPO_DOM 30..749
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..245
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..354
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 393..497
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 498..609
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 615..723
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZE55"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 780..876
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230163"
FT /id="VSP_008706"
FT VARIANT 7
FT /note="W -> R (in dbSNP:rs3742301)"
FT /evidence="ECO:0000269|PubMed:12884975"
FT /id="VAR_017171"
FT VARIANT 39
FT /note="E -> A (in dbSNP:rs5030683)"
FT /evidence="ECO:0000269|PubMed:12884975"
FT /id="VAR_017172"
FT VARIANT 367
FT /note="T -> A (in dbSNP:rs9596693)"
FT /id="VAR_059191"
FT VARIANT 743
FT /note="V -> A (in dbSNP:rs5030685)"
FT /evidence="ECO:0000269|PubMed:12884975"
FT /id="VAR_017173"
FT VARIANT 956
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036108"
FT CONFLICT 39
FT /note="E -> K (in Ref. 2; AAK21986)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="S -> C (in Ref. 5; AAH36025)"
FT /evidence="ECO:0000305"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 500..509
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:6VFV"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:6VFV"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:6VFV"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:6VFV"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:6VFV"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 573..582
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 618..626
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:6VFV"
FT HELIX 644..647
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 649..659
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:6VFV"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 670..673
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 685..695
FT /evidence="ECO:0007829|PDB:6VFV"
FT STRAND 701..711
FT /evidence="ECO:0007829|PDB:6VFV"
SQ SEQUENCE 1070 AA; 113019 MW; CBCCE3C43C0E02D8 CRC64;
MSPVRRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGQAP QCVLAFDVVS FSQEQFRLVH
VEVEVRDVND HAPRFPRAQI PVEVSEGAAV GTRIPLEVPV DEDVGANGLQ TVRLAEPHSP
FRVELQTRAD GAQCADLVLL QELDRESQAA YSLELVAQDG GRPPRSATAA LSVRVLDAND
HSPAFPQGAV AEVELAEDAP VGSLLLDLDA ADPDEGPNGD VVFAFGARTP PEARRLFRLD
PRSGRLTLAG PVDYERQDTY ELDVRAQDRG PGPRAATCKV IVRIRDVNDN APDIAITPLA
APGAPATSPF AAAAAAAALG GADASSPAGA GTPEAGATSL VPEGAARESL VALVSTSDRD
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGAPPLRTV
RPYTVRVGDE NDNAPLFTRP VYEVSVRENN PPGAYLATVA ARDRDLGRNG QVTYRLLEAE
VGRAGGAVST YVSVDPATGA IYALRSFDYE TLRQLDVRIQ ASDGGSPQLS SSALVQVRVL
DQNDHAPVLV HPAPANGSLE VAVPGRTAKD TVVARVQARD ADEGANGELA FELQQQEPRE
AFAIGRRTGE ILLTGDLSQE PPGRVFRALL VISDGGRPPL TTTATVSFVV TAGGGRGPAA
PASAGSPERS RPPGSRLGVS GSVLQWDTPL IVIIVLAGSC TLLLAAIIAI ATTCNRRKKE
VRKGGALREE RPGAAGGGAS APGSPEEAAR GAGPRPNMFD VLTFPGTGKA PFGSPAADAP
PPAVAAAEVP GSEGGSATGE SACHFEGQQR LRGAHAEPYG ASPGFGKEPA PPVAVWKGHS
FNTISGREAE KFSGKDSGKG DSDFNDSDSD ISGDALKKDL INHMQSGLWA CTAECKILGH
SDRCWSPSCS GPNAHPSPHP PAQMSTFCKS TSLPRDPLRR DNYYQAQLPK TVGLQSVYEK
VLHRDYDRTV TLLSPPRPGR LPDLQEIGVP LYQSPPGRYL SPKKGANENV
