CPVL_HUMAN
ID CPVL_HUMAN Reviewed; 476 AA.
AC Q9H3G5; A4D1A4; Q6UX20; Q8NBL7; Q96AR7; Q9HB41;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Probable serine carboxypeptidase CPVL;
DE EC=3.4.16.-;
DE AltName: Full=Carboxypeptidase, vitellogenic-like;
DE AltName: Full=Vitellogenic carboxypeptidase-like protein;
DE Short=VCP-like protein;
DE Short=hVLP;
DE Flags: Precursor;
GN Name=CPVL; Synonyms=VLP; ORFNames=PSEC0124, UNQ197/PRO223;
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], AND VARIANT HIS-398.
RX PubMed=11401439; DOI=10.1006/geno.2000.6484;
RA Mahoney J.A., Ntolosi B., DaSilva R.P., Gordon S., McKnight A.J.;
RT "Cloning and characterization of CPVL, a novel serine carboxypeptidase,
RT from human macrophages.";
RL Genomics 72:243-251(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-25 AND HIS-398.
RA Cho J.-J., Baik H.-H.;
RT "Cloning of VCP-like protein expressed in human heart and placenta.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-435.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-435.
RC TISSUE=Lung;
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-81; ASN-132 AND ASN-346.
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 [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 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 [11]
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 -!- FUNCTION: May be involved in the digestion of phagocytosed particles in
CC the lysosome, participation in an inflammatory protease cascade, and
CC trimming of peptides for antigen presentation.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages but not in other
CC leukocytes. Abundantly expressed in heart and kidney. Also expressed in
CC spleen, leukocytes, and placenta.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AF106704; AAG37991.2; -; mRNA.
DR EMBL; AF282617; AAG14348.1; -; mRNA.
DR EMBL; AY358549; AAQ88913.1; -; mRNA.
DR EMBL; AK075433; BAC11618.1; -; mRNA.
DR EMBL; CH236948; EAL24207.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93914.1; -; Genomic_DNA.
DR EMBL; BC016838; AAH16838.1; -; mRNA.
DR CCDS; CCDS5419.1; -.
DR RefSeq; NP_001334981.1; NM_001348052.1.
DR RefSeq; NP_001334983.1; NM_001348054.1.
DR RefSeq; NP_061902.2; NM_019029.3.
DR RefSeq; NP_112601.3; NM_031311.4.
DR RefSeq; XP_011513739.1; XM_011515437.1.
DR AlphaFoldDB; Q9H3G5; -.
DR SMR; Q9H3G5; -.
DR BioGRID; 120000; 136.
DR IntAct; Q9H3G5; 87.
DR MINT; Q9H3G5; -.
DR STRING; 9606.ENSP00000387164; -.
DR ESTHER; human-CPVL; Carboxypeptidase_S10.
DR MEROPS; S10.003; -.
DR GlyConnect; 1630; 11 N-Linked glycans (3 sites).
DR GlyGen; Q9H3G5; 5 sites, 16 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9H3G5; -.
DR PhosphoSitePlus; Q9H3G5; -.
DR BioMuta; CPVL; -.
DR DMDM; 67476930; -.
DR EPD; Q9H3G5; -.
DR jPOST; Q9H3G5; -.
DR MassIVE; Q9H3G5; -.
DR MaxQB; Q9H3G5; -.
DR PaxDb; Q9H3G5; -.
DR PeptideAtlas; Q9H3G5; -.
DR PRIDE; Q9H3G5; -.
DR ProteomicsDB; 80708; -.
DR Antibodypedia; 26062; 200 antibodies from 28 providers.
DR DNASU; 54504; -.
DR Ensembl; ENST00000265394.10; ENSP00000265394.5; ENSG00000106066.15.
DR Ensembl; ENST00000396276.7; ENSP00000379572.3; ENSG00000106066.15.
DR Ensembl; ENST00000409850.5; ENSP00000387164.1; ENSG00000106066.15.
DR GeneID; 54504; -.
DR KEGG; hsa:54504; -.
DR MANE-Select; ENST00000265394.10; ENSP00000265394.5; NM_031311.5; NP_112601.3.
DR UCSC; uc003szv.4; human.
DR CTD; 54504; -.
DR DisGeNET; 54504; -.
DR GeneCards; CPVL; -.
DR HGNC; HGNC:14399; CPVL.
DR HPA; ENSG00000106066; Tissue enhanced (lymphoid).
DR MIM; 609780; gene.
DR neXtProt; NX_Q9H3G5; -.
DR OpenTargets; ENSG00000106066; -.
DR PharmGKB; PA26850; -.
DR VEuPathDB; HostDB:ENSG00000106066; -.
DR eggNOG; KOG1282; Eukaryota.
DR GeneTree; ENSGT00940000159498; -.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; Q9H3G5; -.
DR OMA; PFHDLDK; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9H3G5; -.
DR TreeFam; TF354323; -.
DR PathwayCommons; Q9H3G5; -.
DR SignaLink; Q9H3G5; -.
DR BioGRID-ORCS; 54504; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; CPVL; human.
DR GeneWiki; CPVL; -.
DR GenomeRNAi; 54504; -.
DR Pharos; Q9H3G5; Tbio.
DR PRO; PR:Q9H3G5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H3G5; protein.
DR Bgee; ENSG00000106066; Expressed in monocyte and 178 other tissues.
DR ExpressionAtlas; Q9H3G5; baseline and differential.
DR Genevisible; Q9H3G5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000004280"
FT CHAIN ?..476
FT /note="Probable serine carboxypeptidase CPVL"
FT /id="PRO_0000004281"
FT ACT_SITE 204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 11
FT /note="S -> L (in dbSNP:rs36074676)"
FT /id="VAR_048681"
FT VARIANT 25
FT /note="R -> H (in dbSNP:rs34219043)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_048682"
FT VARIANT 398
FT /note="R -> H (in dbSNP:rs1052200)"
FT /evidence="ECO:0000269|PubMed:11401439, ECO:0000269|Ref.2"
FT /id="VAR_048683"
FT VARIANT 435
FT /note="A -> V (in dbSNP:rs7313)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16303743"
FT /id="VAR_022612"
FT CONFLICT 284
FT /note="F -> L (in Ref. 1; AAG37991 and 2; AAG14348)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="F -> L (in Ref. 4; BAC11618)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="F -> L (in Ref. 2; AAG14348)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="F -> S (in Ref. 2; AAG14348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 54164 MW; 33AA4A7360BF01E1 CRC64;
MVGAMWKVIV SLVLLMPGPC DGLFRSLYRS VSMPPKGDSG QPLFLTPYIE AGKIQKGREL
SLVGPFPGLN MKSYAGFLTV NKTYNSNLFF WFFPAQIQPE DAPVVLWLQG GPGGSSMFGL
FVEHGPYVVT SNMTLRDRDF PWTTTLSMLY IDNPVGTGFS FTDDTHGYAV NEDDVARDLY
SALIQFFQIF PEYKNNDFYV TGESYAGKYV PAIAHLIHSL NPVREVKINL NGIAIGDGYS
DPESIIGGYA EFLYQIGLLD EKQKKYFQKQ CHECIEHIRK QNWFEAFEIL DKLLDGDLTS
DPSYFQNVTG CSNYYNFLRC TEPEDQLYYV KFLSLPEVRQ AIHVGNQTFN DGTIVEKYLR
EDTVQSVKPW LTEIMNNYKV LIYNGQLDII VAAALTERSL MGMDWKGSQE YKKAEKKVWK
IFKSDSEVAG YIRQAGDFHQ VIIRGGGHIL PYDQPLRAFD MINRFIYGKG WDPYVG
