CPNE3_HUMAN
ID CPNE3_HUMAN Reviewed; 537 AA.
AC O75131; A8KA47; Q8IYA1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Copine-3 {ECO:0000305};
DE AltName: Full=Copine III {ECO:0000303|PubMed:11041869, ECO:0000312|HGNC:HGNC:2316};
GN Name=CPNE3 {ECO:0000312|HGNC:HGNC:2316};
GN Synonyms=CPN3, KIAA0636 {ECO:0000303|PubMed:9734811};
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], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND PHOSPHORYLATION.
RX PubMed=11041869; DOI=10.1021/bi001250v;
RA Caudell E.G., Caudell J.J., Tang C.-H., Yu T.-K., Frederick M.J.,
RA Grimm E.A.;
RT "Characterization of human copine III as a phosphoprotein with associated
RT kinase activity.";
RL Biochemistry 39:13034-13043(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-412.
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [5]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=12949241; DOI=10.1189/jlb.0203083;
RA Cowland J.B., Carter D., Bjerregaard M.D., Johnsen A.H., Borregaard N.,
RA Lollike K.;
RT "Tissue expression of copines and isolation of copines I and III from the
RT cytosol of human neutrophils.";
RL J. Leukoc. Biol. 74:379-388(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21087455; DOI=10.1111/j.1742-4658.2010.07935.x;
RA Perestenko P.V., Pooler A.M., Noorbakhshnia M., Gray A., Bauccio C.,
RA Jeffrey McIlhinney R.A.;
RT "Copines-1, -2, -3, -6 and -7 show different calcium-dependent
RT intracellular membrane translocation and targeting.";
RL FEBS J. 277:5174-5189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH ERBB2; RACK1 AND SHC1, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20010870; DOI=10.1038/onc.2009.456;
RA Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R.,
RA Lienhard S., Duss S., Hofsteenge J., Hynes N.E.;
RT "Copine-III interacts with ErbB2 and promotes tumor cell migration.";
RL Oncogene 29:1598-1610(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-197, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in ERBB2-mediated tumor cell migration in response to growth
CC factor heregulin stimulation (PubMed:20010870).
CC {ECO:0000269|PubMed:20010870}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Monomer (PubMed:12949241). Interacts with ERBB2
CC (preferentially with the tyrosine phosphorylated form); this
CC interaction occurs at the cell membrane and is increased in a growth
CC factor heregulin-dependent manner (PubMed:20010870). Interacts with
CC SHC1; this interaction may mediate the binding of CPNE3 with ERBB2
CC (PubMed:20010870). Interacts with RACK1 (PubMed:20010870).
CC {ECO:0000269|PubMed:12949241, ECO:0000269|PubMed:20010870}.
CC -!- INTERACTION:
CC O75131; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-718988, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20010870,
CC ECO:0000269|PubMed:21087455}. Cytoplasm {ECO:0000269|PubMed:12949241,
CC ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}. Cell
CC membrane {ECO:0000269|PubMed:20010870, ECO:0000269|PubMed:21087455}.
CC Cell junction {ECO:0000269|PubMed:20010870}. Cell junction, focal
CC adhesion {ECO:0000269|PubMed:20010870}. Note=Associates to the membrane
CC in a calcium-dependent manner (PubMed:20010870). Translocates to the
CC cell membrane and the nucleus in a calcium- or growth factor heregulin-
CC dependent manner (PubMed:21087455, PubMed:20010870). Colocalizes with
CC the tyrosine phosphorylated ERBB2 form at cell membrane and focal
CC adhesions in a calcium- or growth factor heregulin-dependent manner
CC (PubMed:20010870). {ECO:0000269|PubMed:20010870,
CC ECO:0000269|PubMed:21087455}.
CC -!- TISSUE SPECIFICITY: Expressed in breast and weakly in prostate and
CC ovarian tissues (PubMed:20010870). Expressed in neutrophils (at protein
CC level) (PubMed:12949241). Widely expressed (PubMed:11041869). Expressed
CC in the brain. Expressed in neutrophil precursors from the bone marrow
CC and peripheral blood (PubMed:12949241). Expressed in primary breast
CC tumors and ovarian endometrioid adenocarcinoma (PubMed:20010870).
CC {ECO:0000269|PubMed:11041869, ECO:0000269|PubMed:12949241,
CC ECO:0000269|PubMed:20010870}.
CC -!- PTM: Phosphorylated on serine and threonine residues (PubMed:11041869).
CC {ECO:0000269|PubMed:11041869}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
CC -!- CAUTION: Was reported to have a protein kinase activity.
CC {ECO:0000305|PubMed:11041869}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31611.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF077226; AAD46074.2; -; mRNA.
DR EMBL; AB014536; BAA31611.2; ALT_INIT; mRNA.
DR EMBL; AK292912; BAF85601.1; -; mRNA.
DR EMBL; BC036242; AAH36242.1; -; mRNA.
DR EMBL; BC066597; AAH66597.1; -; mRNA.
DR CCDS; CCDS6243.1; -.
DR RefSeq; NP_003900.1; NM_003909.4.
DR RefSeq; XP_005251150.1; XM_005251093.4.
DR RefSeq; XP_016869434.1; XM_017013945.1.
DR AlphaFoldDB; O75131; -.
DR SMR; O75131; -.
DR BioGRID; 114412; 73.
DR IntAct; O75131; 22.
DR MINT; O75131; -.
DR STRING; 9606.ENSP00000477590; -.
DR GlyGen; O75131; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75131; -.
DR MetOSite; O75131; -.
DR PhosphoSitePlus; O75131; -.
DR SwissPalm; O75131; -.
DR BioMuta; CPNE3; -.
DR EPD; O75131; -.
DR jPOST; O75131; -.
DR MassIVE; O75131; -.
DR MaxQB; O75131; -.
DR PaxDb; O75131; -.
DR PeptideAtlas; O75131; -.
DR PRIDE; O75131; -.
DR ProteomicsDB; 49793; -.
DR Antibodypedia; 25495; 165 antibodies from 29 providers.
DR DNASU; 8895; -.
DR Ensembl; ENST00000517490.6; ENSP00000477590.1; ENSG00000085719.13.
DR GeneID; 8895; -.
DR KEGG; hsa:8895; -.
DR MANE-Select; ENST00000517490.6; ENSP00000477590.1; NM_003909.5; NP_003900.1.
DR UCSC; uc033bsf.1; human.
DR CTD; 8895; -.
DR DisGeNET; 8895; -.
DR GeneCards; CPNE3; -.
DR HGNC; HGNC:2316; CPNE3.
DR HPA; ENSG00000085719; Low tissue specificity.
DR MIM; 604207; gene.
DR neXtProt; NX_O75131; -.
DR OpenTargets; ENSG00000085719; -.
DR PharmGKB; PA26833; -.
DR VEuPathDB; HostDB:ENSG00000085719; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000154968; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; O75131; -.
DR OMA; EMAAQCV; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; O75131; -.
DR TreeFam; TF316419; -.
DR PathwayCommons; O75131; -.
DR Reactome; R-HSA-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O75131; -.
DR BioGRID-ORCS; 8895; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; CPNE3; human.
DR GenomeRNAi; 8895; -.
DR Pharos; O75131; Tbio.
DR PRO; PR:O75131; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O75131; protein.
DR Bgee; ENSG00000085719; Expressed in tongue squamous epithelium and 209 other tissues.
DR ExpressionAtlas; O75131; baseline and differential.
DR Genevisible; O75131; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0038128; P:ERBB2 signaling pathway; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037768; C2B_Copine.
DR InterPro; IPR045052; Copine.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10857; PTHR10857; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell junction; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..537
FT /note="Copine-3"
FT /id="PRO_0000144838"
FT DOMAIN 1..115
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 124..247
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 291..513
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 252
FT /note="E -> D (in dbSNP:rs41333046)"
FT /id="VAR_048848"
FT VARIANT 412
FT /note="T -> M (in dbSNP:rs2304789)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024424"
FT CONFLICT 394
FT /note="P -> Q (in Ref. 4; AAH36242)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="Q -> R (in Ref. 4; AAH36242)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="R -> H (in Ref. 4; AAH36242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60131 MW; 91F2C5EAD611B842 CRC64;
MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS
KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQIVSSKK LTRPLVMKTG
RPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT
EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
RSSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG
SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE
FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA ATQQQTASQY
FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ
