PCD23_HUMAN
ID PCD23_HUMAN Reviewed; 3371 AA.
AC Q6V1P9; A0A096LNH0; B2RU14; E9PC11; Q4W5P9; Q6ZS61; Q9NXU8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protocadherin-23;
DE AltName: Full=Cadherin-27;
DE AltName: Full=Cadherin-like protein CDHJ;
DE AltName: Full=Cadherin-like protein VR8;
DE AltName: Full=Protein dachsous homolog 2;
DE AltName: Full=Protocadherin PCDHJ;
GN Name=DCHS2; Synonyms=CDH27, CDHJ, PCDH23, PCDHJ;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2357-3371 (ISOFORM 1).
RC TISSUE=Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1244-3371 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=15003449; DOI=10.1016/j.jmb.2004.01.026;
RA Hoeng J.C., Ivanov N.V., Hodor P., Xia M., Wei N., Blevins R., Gerhold D.,
RA Borodovsky M., Liu Y.;
RT "Identification of new human cadherin genes using a combination of protein
RT motif search and gene finding methods.";
RL J. Mol. Biol. 337:307-317(2004).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6V1P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6V1P9-5; Sequence=VSP_060650, VSP_060651;
CC -!- TISSUE SPECIFICITY: Cerebral cortex and testis.
CC {ECO:0000269|PubMed:15003449}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR10443.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAY41019.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA90911.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC87093.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK000054; BAA90911.1; ALT_INIT; mRNA.
DR EMBL; AK127704; BAC87093.1; ALT_FRAME; mRNA.
DR EMBL; AC079298; AAY41019.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC110608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140919; AAI40920.1; -; mRNA.
DR EMBL; AY354497; AAR10443.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47150.1; -. [Q6V1P9-5]
DR CCDS; CCDS87275.1; -. [Q6V1P9-1]
DR RefSeq; NP_001136024.1; NM_001142552.1. [Q6V1P9-5]
DR RefSeq; NP_060109.2; NM_017639.3.
DR RefSeq; XP_011530347.1; XM_011532045.1.
DR SMR; Q6V1P9; -.
DR BioGRID; 120157; 1.
DR IntAct; Q6V1P9; 3.
DR MINT; Q6V1P9; -.
DR STRING; 9606.ENSP00000485514; -.
DR GlyGen; Q6V1P9; 23 sites.
DR iPTMnet; Q6V1P9; -.
DR PhosphoSitePlus; Q6V1P9; -.
DR BioMuta; DCHS2; -.
DR DMDM; 74762378; -.
DR MassIVE; Q6V1P9; -.
DR PaxDb; Q6V1P9; -.
DR PeptideAtlas; Q6V1P9; -.
DR PRIDE; Q6V1P9; -.
DR ProteomicsDB; 19339; -.
DR ProteomicsDB; 67706; -. [Q6V1P9-1]
DR Antibodypedia; 74247; 4 antibodies from 4 providers.
DR DNASU; 54798; -.
DR Ensembl; ENST00000339452.2; ENSP00000345062.1; ENSG00000197410.14. [Q6V1P9-5]
DR Ensembl; ENST00000357232.10; ENSP00000349768.5; ENSG00000197410.14. [Q6V1P9-1]
DR Ensembl; ENST00000639062.3; ENSP00000491252.2; ENSG00000284227.3. [Q6V1P9-1]
DR Ensembl; ENST00000639512.1; ENSP00000492852.1; ENSG00000284227.3. [Q6V1P9-5]
DR GeneID; 54798; -.
DR KEGG; hsa:54798; -.
DR MANE-Select; ENST00000357232.10; ENSP00000349768.5; NM_001358235.2; NP_001345164.1.
DR UCSC; uc003inw.2; human. [Q6V1P9-1]
DR UCSC; uc063aiu.1; human.
DR CTD; 54798; -.
DR DisGeNET; 54798; -.
DR GeneCards; DCHS2; -.
DR HGNC; HGNC:23111; DCHS2.
DR HPA; ENSG00000197410; Tissue enhanced (brain).
DR MIM; 612486; gene.
DR neXtProt; NX_Q6V1P9; -.
DR OpenTargets; ENSG00000197410; -.
DR PharmGKB; PA134953793; -.
DR VEuPathDB; HostDB:ENSG00000197410; -.
DR eggNOG; KOG1219; Eukaryota.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162999; -.
DR HOGENOM; CLU_000265_1_1_1; -.
DR InParanoid; Q6V1P9; -.
DR OMA; PVWEQNP; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; Q6V1P9; -.
DR TreeFam; TF330641; -.
DR PathwayCommons; Q6V1P9; -.
DR SignaLink; Q6V1P9; -.
DR BioGRID-ORCS; 54798; 6 hits in 1078 CRISPR screens.
DR ChiTaRS; DCHS2; human.
DR GeneWiki; DCHS2; -.
DR GenomeRNAi; 54798; -.
DR Pharos; Q6V1P9; Tdark.
DR PRO; PR:Q6V1P9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6V1P9; protein.
DR Bgee; ENSG00000197410; Expressed in prefrontal cortex and 94 other tissues.
DR ExpressionAtlas; Q6V1P9; baseline and differential.
DR Genevisible; Q6V1P9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0072137; P:condensed mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0072006; P:nephron development; IEA:Ensembl.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 24.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 27.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 13.
DR PROSITE; PS50268; CADHERIN_2; 22.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..3371
FT /note="Protocadherin-23"
FT /id="PRO_0000343410"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..2986
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2987..3017
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3018..3371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 65..167
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 168..296
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 297..413
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 424..539
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 540..663
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 664..771
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 772..881
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 877..979
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 980..1082
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1085..1191
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1192..1294
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1299..1415
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1404..1510
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1511..1620
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1620..1724
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1725..1829
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1830..1933
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1934..2038
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2039..2130
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2140..2242
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2243..2347
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2347..2447
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2448..2549
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2550..2665
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2666..2769
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2770..2880
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2881..2988
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3117..3141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3117..3134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2054
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2098
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1340..1369
FT /note="EDSSDHFKIDANNGEIRTTTILSYDYRPSY -> ARPMPLKGKTAFGKQSCK
FT KQTNKQTNKILT (in isoform 2)"
FT /id="VSP_060650"
FT VAR_SEQ 1370..3371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_060651"
FT CONFLICT 15
FT /note="R -> Q (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> G (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="G -> C (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="Q -> E (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="A -> V (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="T -> A (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="H -> R (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="S -> L (in Ref. 3; AAI40920)"
FT /evidence="ECO:0000305"
FT CONFLICT 2516
FT /note="Q -> R (in Ref. 1; BAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 2529
FT /note="L -> P (in Ref. 1; BAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 2930
FT /note="K -> R (in Ref. 1; BAA90911)"
FT /evidence="ECO:0000305"
FT CONFLICT 3088
FT /note="H -> Y (in Ref. 1; BAA90911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3371 AA; 370228 MW; F45D1B281949C90C CRC64;
MSPCGRKMGE GRQQRRAPVG KLLLLPGRRD TPHGRSGSSG ARTQRSLLWL LVHVWLWAAS
GSSAQLFNLT LSVDEGLPPD TLVGDIRAGL PAAQQQEGSG FFLSEDSDDS PLLDDFHVHP
DTGIIRTARR LDRERRDHYS FVAATLLGAV VQVEIRVNDV NDHSPRFPLD SLQLDVSELS
PPGTAFRLPV AHDPDAGLFS TQGYTLVQPS DLPKDPAGPF FQLRYRTPGP LPSPLLPGSS
SPLEPLDLVL LRRLDREEAA AHRLQIEAWD GGRPRRTGLL SVELRVLDEN DNPPVFEQDE
YRAAVREDAQ PGAEVCRVRA TDRDLGPNGF VRYSVRARQV PGAGSGGGAL GDAAYFAVEE
LSGVVRVWRP LDREAQAWHQ LVVEARDGGA EPEVATVRVS IAVLDVNDNR PAIHVLFLTE
GGVARVSEGA RPGDYVARVS VSDADGDWEK EDEATGELGV GLGDGSISLS LEGGEGDFAL
LPGGPPGVFF LCVEGPLDRE SRDLYELLLV ATDAGSPPLS TEETLLLRVA DLNDQPPLFS
QQHYKASVSE AAAPGTVVMW VSASDADEAG SDHAWLRYTV VQLSAPCNLG SLQSKMVHTA
ECGPSFAIDS ESGAISTIRT LDREVQEAVE LKVVAQDLGE PPLSATCLVS ITVDDVNDNE
PIFWRQVYNA TIAEHAPVGH CFLQVTASDA DSGLYGFIEY SLYDGFLSYE APQAFRIDPH
DGQICVSQDI DRERDPATYD LLVEAKDGGG LSAQAFVRVD LEDVNDNHPV FNPSTYVTSI
SDETQPGTEI INVLATDQDS GIYGTVAYEL IPGNVSSLFT IDSTTGIIYL TLPLSHLEST
TLSLMVSAQD GGGLTAVINA DVTIHIFQTT LAPAEFERPK YTFLVYEDVP EDSPIGTVKA
REPLNSSEPI FYRISSGDLG GKFSIHPRLG TIRTRKPLDH ETQPVVVLTV QAQLGSAPAC
SSTEVNITVM DVNDNHPAFL RTSDEIRISQ TTPPGTALYL ARAEDRDSGR NGLIRYSIAS
PQPGVFAIDR ALGVLFLNGS LGAGEQRELT LTLRAEDQGV HPQAALLVLT VVIEKREHSP
SWTFEHLVYQ VEVSESLSPM TQMLQTQAHP LGPQRAASPL RYSLEPSVDS AMFGIRPYTG
WIYLRRQFDY ESTQTYNFRV FAWIPEDGFL QNVSTTVIVR VWDENDNSPT FLHDVLFLKV
EESPVPQGVI GKITAIDMDS GKNGQLLYFL LSDGKFFKMN PNTGELINWV ALDREHRGHH
EMTVLVTDRG SPPRNATMAV YVSVTDINDN RPFFPQCLPG KELHVKVLEG QPVNMLVTTV
FAKDPDEGNN AEVTYSVSSE DSSDHFKIDA NNGEIRTTTI LSYDYRPSYR MSVIATDQGV
PPLQGQAVVN IQVIPLSKGR AIMSQNIRHL IIPENLKPTK IMSLIKSSDH LQQHYNGKLH
FSIVADDKDG HFEIDSSTGD LFLSKELDYE TTSHYLFRVI TTDHSKNLSL SSTVFLSIDV
EDQNDHSPSF QDELIVISVE ENVPIGTLVY VFNAKDDDGS FLNSRIQYYI ESHNPGTNPF
LIHPSFGTLV TVSRLDRESI PTVILTVTAS DQAVNVTDRR LRSLTAQIVI LDVNDHNPTF
ISFPNAHVKE DVTVGSLVHH ITAHDPDEGR NGKVTYSILS GNENMTFMLD ESSGLLTTTC
PLDYEMKTQH ILTVLALDDG TPALSSSQTL TVTVLDVNDE APVFKQHLYE ASVKENQNPG
EFVTRVEALD RDSGVNSKLQ FEIMPGASFE LFEINSDTGE VVTTTILDRE IQEVFTLRVL
VRDGGFPSLS STTTILCTVE DENDHAPEFI VSSYDIEVLE NQEPEVVYTV LASDMDAGNN
RAVEYHIIDG NTDECFTINE MSGELSTTRA LDREQISNFT LVILCSDLGD PPRSSVIHLQ
VRVLDANDHS PSFPTLYYQS SVREDAEVGT VVLVLSAVDK DEGLNGQTEY FLTDEASGAF
TIDPMSGTLK TSNTLDREAR SQHTFSAVAR DCSIQGSRST TVIIKVYVTD VNDNDPVLEQ
NPFDVFLSPE SPTNQTTVIV RADDLDLGPN GTVVFSFAET QSMFSIDKYT GEIQFQQNPS
SEYFPIWLQL KVTDQGIPAR TTTGLLVIHM EGEDVKISFS HHLYKGLVTE NCEAGTSIVT
VKAFAPDSIQ DSMKYSIFSG NEDGVLSLCS KSGQLTVKEP KFLDFEVRNE VQLIVLAESS
GHRAYCKVAV LIQDENDNSP CFEQSIYQAS VSESQLYNAH VIQVFATDLD SGLNGLIEYS
ILSGNQEEAF QIDALSGVIT TKAILDYELT SSYSLIVQAT DKGMPRLSNT TVIKVQVTDI
NDNAPAFLPS EAVEITEDSL PGVIVTHVSV HDVDLNSAFI FSFAKESNPG TKFAIDQNTG
VVVLVKTLDF EEMTEYELLI QISDSVHYTE GALVVRVLDV NDNPPVFSQD FYQVTVPESI
PVGYSVLTLS ATDLESNENI SYRILSSSKE FSIDPKNGTI FTISPVLLLD TISTTQFLVE
ASDGGNPDLR ALTLVEIGIE DMNNYAPEFT VKSYNLSLSE DALVGSTLVT FSNIDHDWTR
ENTYVEYSII SGNSQNNFHV ETKFFHSEYP YKQVGYLVLL HSLDREASAS HELVILASDS
GCPPLSSTAV ISIQVLDVND NPPNFSSLSY HTHVKESTPL GSHITVVSAN DRDTGSHAEI
IYNIISGNEK GHFYLEENTG VLYLIKPLDY EKMTKFTLTV QASDAEKKHF SFAVVFVSVL
DDNDHAPQFM FSSFSCIVPE NLPISSTICS INALDFDAGP YGELTYSIVS PCFLTHGMSY
DHDLFLIDPL TGDIHAKQIL DYENGNKYCL TVQAKDKGDA TASLVVWVDI EGIDEFEPIF
TQDQYFFTLP EKNKDRQLIG RVEASDADAG IDGVILYSLG TSSPFFSVNK TNGNIYLIRA
LPLIKSQLNK EDTLEMKIIA HSPKSDSKFA SCTVFVNVSF SSEGTPLAVF ASSFSISLVV
SFLVFLILIC ILIVMILRHK QKDTINNYEE KKTSSLDADL RVTRDASVLK AFQKTDDCSN
EVVPVDATPE WLSLISIMEK DIVNLYRHSN SSGHCSVEGE TAEDKEIQRI NEHPYRKCSD
SALSDHESRV PDSGIPRDSD QLSCLSGETD VMVTAETAEA SQTFGEGDQG EGCSTTCAQN
NVLPQTVQKR EAKESILADV RKESVFISGD QEVRCAALST QTTSDHDGKD NYHWNYLLSW
EPKFQPLASV FNDIAKLKDE HLHMPGIPKE KKSFVFPPPL ITAVAQPGIK AVPPRMPAVN
LGQVPPKHPR SPIPYHLGSL PEGMTPNFSP SLSLLTMQPP ALSPLLREGE LLGTHISGTC
HELKAEDEVQ I
