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   13-FEB-2019, entry version 172.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   human 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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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
RP   GLU-36; 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
RT   project: 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
RT   multiple 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
RP   AND THR-1370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Buerckstuemmer T., 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
RP   AND THR-1370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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.,
RA   Ayoub D., 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.
CC       {ECO:0000250|UniProtKB:Q90240};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-6.5.;
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane
CC       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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta, pancreas and
CC       hepatoma cells. Lower levels found in skeletal muscle, heart and
CC       colon carcinoma and melanoma cell lines.
CC   -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first
CC       two 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   UniGene; Hs.446079; -.
DR   PDB; 5AQ0; X-ray; 0.95 A; A/B=383-461.
DR   PDBsum; 5AQ0; -.
DR   ProteinModelPortal; O75976; -.
DR   SMR; O75976; -.
DR   BioGrid; 107754; 22.
DR   IntAct; O75976; 12.
DR   MINT; O75976; -.
DR   STRING; 9606.ENSP00000225719; -.
DR   DrugBank; DB04489; Guanidinoethylmercaptosuccinic acid.
DR   MEROPS; M14.011; -.
DR   CarbonylDB; O75976; -.
DR   GlyConnect; 1066; -.
DR   iPTMnet; O75976; -.
DR   PhosphoSitePlus; O75976; -.
DR   SwissPalm; O75976; -.
DR   BioMuta; CPD; -.
DR   EPD; O75976; -.
DR   jPOST; O75976; -.
DR   MaxQB; O75976; -.
DR   PaxDb; O75976; -.
DR   PeptideAtlas; O75976; -.
DR   PRIDE; O75976; -.
DR   ProteomicsDB; 50336; -.
DR   DNASU; 1362; -.
DR   Ensembl; ENST00000225719; ENSP00000225719; ENSG00000108582. [O75976-1]
DR   Ensembl; ENST00000543464; ENSP00000444443; ENSG00000108582. [O75976-2]
DR   GeneID; 1362; -.
DR   KEGG; hsa:1362; -.
DR   UCSC; uc002hfb.3; human. [O75976-1]
DR   CTD; 1362; -.
DR   DisGeNET; 1362; -.
DR   EuPathDB; HostDB:ENSG00000108582.11; -.
DR   GeneCards; CPD; -.
DR   HGNC; HGNC:2301; CPD.
DR   HPA; HPA052796; -.
DR   HPA; HPA055465; -.
DR   MIM; 603102; gene.
DR   neXtProt; NX_O75976; -.
DR   OpenTargets; ENSG00000108582; -.
DR   PharmGKB; PA26823; -.
DR   eggNOG; KOG2649; Eukaryota.
DR   eggNOG; ENOG410XX0H; LUCA.
DR   GeneTree; ENSGT00940000156919; -.
DR   HOGENOM; HOG000046445; -.
DR   HOVERGEN; HBG006932; -.
DR   InParanoid; O75976; -.
DR   KO; K07752; -.
DR   OMA; DFRHHHF; -.
DR   OrthoDB; 101221at2759; -.
DR   PhylomeDB; O75976; -.
DR   TreeFam; TF315592; -.
DR   BRENDA; 3.4.17.22; 2681.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   ChiTaRS; CPD; human.
DR   GeneWiki; CPD_(gene); -.
DR   GenomeRNAi; 1362; -.
DR   PRO; PR:O75976; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000108582; Expressed in 233 organ(s), highest expression level in parotid gland.
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; cd03868; M14_CPD_I; 1.
DR   CDD; cd03863; M14_CPD_II; 1.
DR   CDD; cd06245; M14_CPD_III; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR034241; M14_CPD_I.
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   Complete proteome; Glycoprotein; Hydrolase; Lipoprotein; Membrane;
KW   Metal-binding; Metalloprotease; Palmitate; Phosphoprotein;
KW   Polymorphism; Protease; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32   1380       Carboxypeptidase D.
FT                                /FTId=PRO_0000004401.
FT   TOPO_DOM     32   1299       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1300   1320       Helical. {ECO:0000255}.
FT   TOPO_DOM   1321   1380       Cytoplasmic. {ECO:0000255}.
FT   REGION       32    493       Carboxypeptidase-like 1.
FT   REGION      494    897       Carboxypeptidase-like 2.
FT   REGION      898   1299       Carboxypeptidase-like 3.
FT   MOTIF       162    164       Cell attachment site. {ECO:0000255}.
FT   ACT_SITE    762    762       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:P14384}.
FT   METAL       139    139       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P19222}.
FT   METAL       142    142       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P19222}.
FT   METAL       257    257       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P19222}.
FT   METAL       564    564       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P00730}.
FT   METAL       567    567       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P00730}.
FT   METAL       671    671       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P00730}.
FT   MOD_RES     265    265       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O89001}.
FT   MOD_RES     270    270       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O89001}.
FT   MOD_RES    1358   1358       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1361   1361       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1368   1368       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1370   1370       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   LIPID      1317   1317       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:12643288}.
FT   LIPID      1321   1321       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:12643288}.
FT   LIPID      1323   1323       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:12643288}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    399    399       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    429    429       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    522    522       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    626    626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    811    811       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    855    855       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    867    867       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    879    879       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    955    955       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    978    978       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1070   1070       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1142   1142       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ       1      2       MA -> MR (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045833.
FT   VAR_SEQ       3    249       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045834.
FT   VARIANT      36     36       K -> E (in dbSNP:rs17857300).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_027771.
FT   VARIANT     454    454       E -> G (in dbSNP:rs17857301).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_027772.
FT   VARIANT     505    505       H -> N (in dbSNP:rs17854355).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_027773.
FT   VARIANT     899    899       T -> I (in dbSNP:rs1860543).
FT                                /FTId=VAR_027774.
FT   CONFLICT    863    863       A -> V (in Ref. 3; BAH14780).
FT                                {ECO:0000305}.
FT   CONFLICT    896    896       D -> V (in Ref. 1 and 2). {ECO:0000305}.
FT   CONFLICT    948    948       M -> I (in Ref. 3; BAH14780).
FT                                {ECO:0000305}.
FT   CONFLICT   1336   1336       R -> W (in Ref. 3; BAH13725).
FT                                {ECO:0000305}.
FT   STRAND      383    390       {ECO:0000244|PDB:5AQ0}.
FT   TURN        391    393       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      401    404       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      417    422       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      425    433       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      440    447       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      449    451       {ECO:0000244|PDB:5AQ0}.
FT   STRAND      457    459       {ECO:0000244|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
//