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   27-MAR-2024, entry version 200.
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; 223.
DR   IntAct; O75976; 50.
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   GlyCosmos; O75976; 25 sites, 29 glycans.
DR   GlyGen; O75976; 35 sites, 23 N-linked glycans (7 sites), 7 O-linked glycans (14 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; 9606-ENSP00000225719; -.
DR   PeptideAtlas; O75976; -.
DR   ProteomicsDB; 25034; -.
DR   ProteomicsDB; 50336; -. [O75976-1]
DR   Pumba; O75976; -.
DR   Antibodypedia; 26863; 125 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   AGR; HGNC:2301; -.
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; QAAHIKK; -.
DR   OrthoDB; 5490979at2759; -.
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; 64 hits in 1171 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 214 other cell types or tissues.
DR   ExpressionAtlas; O75976; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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   CDD; cd11308; Peptidase_M14NE-CP-C_like; 3.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 3.
DR   Gene3D; 3.40.630.10; Zn peptidases; 3.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR034224; M14_CPD_II.
DR   InterPro; IPR033848; M14_CPD_III.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF73; CARBOXYPEPTIDASE D; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 3.
DR   Pfam; PF00246; Peptidase_M14; 3.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 3.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 3.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 3.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
DR   PROSITE; PS52035; PEPTIDASE_M14; 3.
DR   Genevisible; O75976; HS.
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   DOMAIN          57..380
FT                   /note="Peptidase M14 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   DOMAIN          502..792
FT                   /note="Peptidase M14 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   DOMAIN          932..1211
FT                   /note="Peptidase M14 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   REGION          190..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        350
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   ACT_SITE        762
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT   BINDING         671
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
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
//