CBPD_HUMAN
ID CBPD_HUMAN Reviewed; 1380 AA.
AC O75976; B7Z7T9; B7ZAU4; F5GZH6; O15377; Q86SH9; Q86XE6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=Metallocarboxypeptidase D;
DE AltName: Full=gp180;
DE Flags: Precursor;
GN Name=CPD;
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).
RC TISSUE=Fetal liver;
RX PubMed=9714835; DOI=10.1016/s0378-1119(98)00270-4;
RA Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F.,
RA Kuroki K.;
RT "Cloning, functional expression, and chromosomal localization of the human
RT and mouse gp180-carboxypeptidase D-like enzyme.";
RL Gene 215:361-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain, and Placenta;
RX PubMed=9355738; DOI=10.1042/bj3270081;
RA Tan F., Rehli M., Krause S.W., Skidgel R.A.;
RT "Sequence of human carboxypeptidase D reveals it to be a member of the
RT regulatory carboxypeptidase family with three tandem active site domains.";
RL Biochem. J. 327:81-87(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP SEQUENCE REVISION TO 11-13; 49-52; 159-162 AND 493.
RA Tan F., Rehli M., Skidgel R.A.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-36;
RP GLY-454 AND ASN-505.
RC TISSUE=Testis;
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 [7]
RP CHARACTERIZATION.
RX PubMed=9064476; DOI=10.1016/s0024-3205(96)00642-x;
RA McGwire G.B., Tan F., Michel B., Rehli M., Skidgel R.A.;
RT "Identification of a membrane-bound carboxypeptidase as the mammalian
RT homolog of duck gp180, a hepatitis B virus-binding protein.";
RL Life Sci. 60:715-724(1997).
RN [8]
RP PALMITOYLATION AT CYS-1317; CYS-1321 AND CYS-1323.
RX PubMed=12643288; DOI=10.1074/jbc.m209379200;
RA Kalinina E.V., Fricker L.D.;
RT "Palmitoylation of carboxypeptidase D. Implications for intracellular
RT trafficking.";
RL J. Biol. Chem. 278:9244-9249(2003).
RN [9]
RP GLYCOSYLATION AT ASN-172; ASN-811 AND ASN-955.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1368 AND THR-1370, AND
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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811; ASN-955 AND ASN-1070.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358; SER-1361; THR-1368 AND
RP THR-1370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358; SER-1361; THR-1368 AND
RP THR-1370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1368 AND THR-1370, 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 [16]
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).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q90240};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5.;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75976-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75976-2; Sequence=VSP_045833, VSP_045834;
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, pancreas and hepatoma
CC cells. Lower levels found in skeletal muscle, heart and colon carcinoma
CC and melanoma cell lines.
CC -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first two
CC domains seem to have kept a catalytic activity.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; D85390; BAA33370.1; -; mRNA.
DR EMBL; U65090; AAC51775.2; -; mRNA.
DR EMBL; AK302497; BAH13725.1; -; mRNA.
DR EMBL; AK316409; BAH14780.1; -; mRNA.
DR EMBL; AC006050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045549; AAH45549.1; -; mRNA.
DR EMBL; BC045624; AAH45624.1; -; mRNA.
DR EMBL; BC051702; AAH51702.1; -; mRNA.
DR CCDS; CCDS11257.1; -. [O75976-1]
DR CCDS; CCDS56025.1; -. [O75976-2]
DR RefSeq; NP_001186704.1; NM_001199775.1. [O75976-2]
DR RefSeq; NP_001295.2; NM_001304.4. [O75976-1]
DR PDB; 5AQ0; X-ray; 0.95 A; A/B=383-461.
DR PDBsum; 5AQ0; -.
DR AlphaFoldDB; O75976; -.
DR SMR; O75976; -.
DR BioGRID; 107754; 193.
DR IntAct; O75976; 30.
DR MINT; O75976; -.
DR STRING; 9606.ENSP00000225719; -.
DR ChEMBL; CHEMBL4523154; -.
DR DrugBank; DB04489; Guanidinoethylmercaptosuccinic acid.
DR MEROPS; M14.011; -.
DR MEROPS; M14.016; -.
DR MEROPS; M14.950; -.
DR CarbonylDB; O75976; -.
DR GlyConnect; 1066; 24 N-Linked glycans (7 sites).
DR GlyGen; O75976; 31 sites, 23 N-linked glycans (7 sites), 6 O-linked glycans (10 sites).
DR iPTMnet; O75976; -.
DR MetOSite; O75976; -.
DR PhosphoSitePlus; O75976; -.
DR SwissPalm; O75976; -.
DR BioMuta; CPD; -.
DR EPD; O75976; -.
DR jPOST; O75976; -.
DR MassIVE; O75976; -.
DR MaxQB; O75976; -.
DR PaxDb; O75976; -.
DR PeptideAtlas; O75976; -.
DR PRIDE; O75976; -.
DR ProteomicsDB; 25034; -.
DR ProteomicsDB; 50336; -. [O75976-1]
DR Antibodypedia; 26863; 106 antibodies from 26 providers.
DR DNASU; 1362; -.
DR Ensembl; ENST00000225719.9; ENSP00000225719.4; ENSG00000108582.12. [O75976-1]
DR Ensembl; ENST00000543464.6; ENSP00000444443.2; ENSG00000108582.12. [O75976-2]
DR GeneID; 1362; -.
DR KEGG; hsa:1362; -.
DR MANE-Select; ENST00000225719.9; ENSP00000225719.4; NM_001304.5; NP_001295.2.
DR UCSC; uc002hfb.3; human. [O75976-1]
DR CTD; 1362; -.
DR DisGeNET; 1362; -.
DR GeneCards; CPD; -.
DR HGNC; HGNC:2301; CPD.
DR HPA; ENSG00000108582; Low tissue specificity.
DR MIM; 603102; gene.
DR neXtProt; NX_O75976; -.
DR OpenTargets; ENSG00000108582; -.
DR PharmGKB; PA26823; -.
DR VEuPathDB; HostDB:ENSG00000108582; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156919; -.
DR HOGENOM; CLU_002495_1_0_1; -.
DR InParanoid; O75976; -.
DR OMA; DLWVMEI; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; O75976; -.
DR TreeFam; TF315592; -.
DR BRENDA; 3.4.17.22; 2681.
DR PathwayCommons; O75976; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; O75976; -.
DR BioGRID-ORCS; 1362; 61 hits in 1092 CRISPR screens.
DR ChiTaRS; CPD; human.
DR GeneWiki; CPD_(gene); -.
DR GenomeRNAi; 1362; -.
DR Pharos; O75976; Tbio.
DR PRO; PR:O75976; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75976; protein.
DR Bgee; ENSG00000108582; Expressed in parotid gland and 212 other tissues.
DR ExpressionAtlas; O75976; baseline and differential.
DR Genevisible; O75976; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd03863; M14_CPD_II; 1.
DR CDD; cd06245; M14_CPD_III; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034224; M14_CPD_II.
DR InterPro; IPR033848; M14_CPD_III.
DR InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF73; PTHR11532:SF73; 3.
DR Pfam; PF00246; Peptidase_M14; 3.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 3.
DR SUPFAM; SSF49464; SSF49464; 3.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane;
KW Glycoprotein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Palmitate; Phosphoprotein; Protease; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1380
FT /note="Carboxypeptidase D"
FT /id="PRO_0000004401"
FT TOPO_DOM 32..1299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1300..1320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1321..1380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..493
FT /note="Carboxypeptidase-like 1"
FT REGION 190..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..897
FT /note="Carboxypeptidase-like 2"
FT REGION 874..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..1299
FT /note="Carboxypeptidase-like 3"
FT REGION 1359..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 162..164
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 762
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O89001"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89001"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT LIPID 1317
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12643288"
FT LIPID 1321
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12643288"
FT LIPID 1323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12643288"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..2
FT /note="MA -> MR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045833"
FT VAR_SEQ 3..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045834"
FT VARIANT 36
FT /note="K -> E (in dbSNP:rs17857300)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027771"
FT VARIANT 454
FT /note="E -> G (in dbSNP:rs17857301)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027772"
FT VARIANT 505
FT /note="H -> N (in dbSNP:rs17854355)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027773"
FT VARIANT 899
FT /note="T -> I (in dbSNP:rs1860543)"
FT /id="VAR_027774"
FT CONFLICT 863
FT /note="A -> V (in Ref. 3; BAH14780)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="D -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="M -> I (in Ref. 3; BAH14780)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336
FT /note="R -> W (in Ref. 3; BAH13725)"
FT /evidence="ECO:0000305"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:5AQ0"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:5AQ0"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:5AQ0"
SQ SEQUENCE 1380 AA; 152931 MW; 567EC1F0B4B7A0C8 CRC64;
MASGRDERPP WRLGRLLLLM CLLLLGSSAR AAHIKKAEAT TTTTSAGAEA AEGQFDRYYH
EEELESALRE AAAAGLPGLA RLFSIGRSVE GRPLWVLRLT AGLGSLIPEG DAGPDAAGPD
AAGPLLPGRP QVKLVGNMHG DETVSRQVLI YLARELAAGY RRGDPRLVRL LNTTDVYLLP
SLNPDGFERA REGDCGFGDG GPSGASGRDN SRGRDLNRSF PDQFSTGEPP ALDEVPEVRA
LIEWIRRNKF VLSGNLHGGS VVASYPFDDS PEHKATGIYS KTSDDEVFKY LAKAYASNHP
IMKTGEPHCP GDEDETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE LSCCKYPPAS
QLRQEWENNR ESLITLIEKV HIGVKGFVKD SITGSGLENA TISVAGINHN ITTGRFGDFY
RLLVPGTYNL TVVLTGYMPL TVTNVVVKEG PATEVDFSLR PTVTSVIPDT TEAVSTASTV
AIPNILSGTS SSYQPIQPKD FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV
MEISDNPGVH EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVHNTRI
HLMPSMNPDG YEKSQEGDSI SVIGRNNSNN FDLNRNFPDQ FVQITDPTQP ETIAVMSWMK
SYPFVLSANL HGGSLVVNYP FDDDEQGLAT YSKSPDDAVF QQIALSYSKE NSQMFQGRPC
KNMYPNEYFP HGITNGASWY NVPGGMQDWN YLQTNCFEVT IELGCVKYPL EKELPNFWEQ
NRRSLIQFMK QVHQGVRGFV LDATDGRGIL NATISVAEIN HPVTTYKTGD YWRLLVPGTY
KITASARGYN PVTKNVTVKS EGAIQVNFTL VRSSTDSNNE SKKGKGASSS TNDASDPTTK
EFETLIKDLS AENGLESLML RSSSNLALAL YRYHSYKDLS EFLRGLVMNY PHITNLTNLG
QSTEYRHIWS LEISNKPNVS EPEEPKIRFV AGIHGNAPVG TELLLALAEF LCLNYKKNPA
VTQLVDRTRI VIVPSLNPDG RERAQEKDCT SKIGQTNARG KDLDTDFTNN ASQPETKAII
ENLIQKQDFS LSVALDGGSM LVTYPYDKPV QTVENKETLK HLASLYANNH PSMHMGQPSC
PNKSDENIPG GVMRGAEWHS HLGSMKDYSV TYGHCPEITV YTSCCYFPSA ARLPSLWADN
KRSLLSMLVE VHKGVHGFVK DKTGKPISKA VIVLNEGIKV QTKEGGYFHV LLAPGVHNII
AIADGYQQQH SQVFVHHDAA SSVVIVFDTD NRIFGLPREL VVTVSGATMS ALILTACIIW
CICSIKSNRH KDGFHRLRQH HDEYEDEIRM MSTGSKKSLL SHEFQDETDT EEETLYSSKH
