PCOC1_HUMAN
ID PCOC1_HUMAN Reviewed; 449 AA.
AC Q15113; B2R9E1; O14550;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Procollagen C-endopeptidase enhancer 1;
DE AltName: Full=Procollagen COOH-terminal proteinase enhancer 1;
DE Short=PCPE-1;
DE Short=Procollagen C-proteinase enhancer 1;
DE AltName: Full=Type 1 procollagen C-proteinase enhancer protein;
DE AltName: Full=Type I procollagen COOH-terminal proteinase enhancer;
DE Flags: Precursor;
GN Name=PCOLCE; Synonyms=PCPE1;
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].
RC TISSUE=Placenta;
RX PubMed=7523404; DOI=10.1016/s0021-9258(18)47191-8;
RA Takahara K., Kessler E., Biniaminov L., Brusel M., Eddy R.L., Jani-Sait S.,
RA Shows T.B., Greenspan D.S.;
RT "Type I procollagen COOH-terminal proteinase enhancer protein:
RT identification, primary structure, and chromosomal localization of the
RT cognate human gene (PCOLCE).";
RL J. Biol. Chem. 269:26280-26285(1994).
RN [2]
RP SEQUENCE REVISION TO 56; 154 AND 373.
RA Kessler E.;
RL Submitted (FEB-2000) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Hirahara I., Syoufuda K., Harada K., Tomita M., Urakami K., Terai H.,
RA Morisaki N., Saito Y.;
RT "Smooth muscle cell derived procollagen C-protease enhancer protein.";
RL Cell Struct. Funct. 21:662-662(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA Tsui L.-C., Rosenthal A.;
RT "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT genes.";
RL Genome Res. 8:1060-1073(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9933570; DOI=10.1006/geno.1998.5663;
RA Scott I.C., Clark T.G., Takahara K., Hoffman G.G., Greenspan D.S.;
RT "Structural organization and expression patterns of the human and mouse
RT genes for the type I procollagen COOH-terminal proteinase enhancer
RT protein.";
RL Genomics 55:229-234(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [9]
RP PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION OF INHIBITORY ACTIVITY, AND
RP CLEAVAGE SITE.
RX PubMed=10625689; DOI=10.1074/jbc.275.2.1384;
RA Mott J.D., Thomas C.L., Rosenbach M.T., Takahara K., Greenspan D.S.,
RA Banda M.J.;
RT "Post-translational proteolytic processing of procollagen C-terminal
RT proteinase enhancer releases a metalloproteinase inhibitor.";
RL J. Biol. Chem. 275:1384-1390(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [11]
RP STRUCTURE BY NMR OF 313-442, AND DISULFIDE BONDS.
RX PubMed=12670942; DOI=10.1074/jbc.m302734200;
RA Liepinsh E., Banyai L., Pintacuda G., Trexler M., Patthy L., Otting G.;
RT "NMR structure of the netrin-like domain (NTR) of human type I procollagen
RT C-proteinase enhancer defines structural consensus of NTR domains and
RT assesses potential proteinase inhibitory activity and ligand binding.";
RL J. Biol. Chem. 278:25982-25989(2003).
CC -!- FUNCTION: Binds to the C-terminal propeptide of type I procollagen and
CC enhances procollagen C-proteinase activity.
CC -!- FUNCTION: C-terminal processed part of PCPE (CT-PCPE) may have an
CC metalloproteinase inhibitory activity.
CC -!- SUBUNIT: Interacts with EFEMP2. {ECO:0000250|UniProtKB:Q61398}.
CC -!- INTERACTION:
CC Q15113; PRO_0000000092 [P05067]: APP; NbExp=4; IntAct=EBI-8869614, EBI-821758;
CC Q15113; P13497: BMP1; NbExp=3; IntAct=EBI-8869614, EBI-489827;
CC Q15113; PRO_0000005794 [P39060]: COL18A1; NbExp=4; IntAct=EBI-8869614, EBI-2566375;
CC Q15113; P20908: COL5A1; NbExp=2; IntAct=EBI-8869614, EBI-2464511;
CC Q15113; P07996: THBS1; NbExp=3; IntAct=EBI-8869614, EBI-2530274;
CC Q15113; P07589: FN1; Xeno; NbExp=2; IntAct=EBI-8869614, EBI-11147184;
CC Q15113; P18828: Sdc1; Xeno; NbExp=4; IntAct=EBI-8869614, EBI-9985816;
CC Q15113; P43407: Sdc2; Xeno; NbExp=4; IntAct=EBI-8869614, EBI-11578890;
CC Q15113; O35988: Sdc4; Xeno; NbExp=2; IntAct=EBI-8869614, EBI-9986850;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: C-terminally processed at multiple positions.
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DR EMBL; L33799; AAA61949.1; ALT_SEQ; mRNA.
DR EMBL; AB008549; BAA23281.1; -; mRNA.
DR EMBL; AF053356; AAC78800.1; -; Genomic_DNA.
DR EMBL; AF083655; AAD16041.1; -; Genomic_DNA.
DR EMBL; AK313748; BAG36488.1; -; mRNA.
DR EMBL; CH471091; EAW76515.1; -; Genomic_DNA.
DR EMBL; BC000574; AAH00574.1; -; mRNA.
DR EMBL; BC033205; AAH33205.1; -; mRNA.
DR CCDS; CCDS5700.1; -.
DR PIR; A55362; A55362.
DR RefSeq; NP_002584.2; NM_002593.3.
DR PDB; 1UAP; NMR; -; A=313-442.
DR PDB; 6FZV; X-ray; 2.70 A; D=26-278.
DR PDB; 6FZW; X-ray; 2.78 A; D=26-278.
DR PDBsum; 1UAP; -.
DR PDBsum; 6FZV; -.
DR PDBsum; 6FZW; -.
DR AlphaFoldDB; Q15113; -.
DR BMRB; Q15113; -.
DR SASBDB; Q15113; -.
DR SMR; Q15113; -.
DR BioGRID; 111147; 4.
DR IntAct; Q15113; 24.
DR MINT; Q15113; -.
DR STRING; 9606.ENSP00000223061; -.
DR GlyGen; Q15113; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15113; -.
DR PhosphoSitePlus; Q15113; -.
DR BioMuta; PCOLCE; -.
DR DMDM; 6919941; -.
DR EPD; Q15113; -.
DR jPOST; Q15113; -.
DR MassIVE; Q15113; -.
DR MaxQB; Q15113; -.
DR PaxDb; Q15113; -.
DR PeptideAtlas; Q15113; -.
DR PRIDE; Q15113; -.
DR ProteomicsDB; 60442; -.
DR Antibodypedia; 4318; 274 antibodies from 33 providers.
DR DNASU; 5118; -.
DR Ensembl; ENST00000223061.6; ENSP00000223061.5; ENSG00000106333.13.
DR GeneID; 5118; -.
DR KEGG; hsa:5118; -.
DR MANE-Select; ENST00000223061.6; ENSP00000223061.5; NM_002593.4; NP_002584.2.
DR UCSC; uc003uvo.5; human.
DR CTD; 5118; -.
DR DisGeNET; 5118; -.
DR GeneCards; PCOLCE; -.
DR HGNC; HGNC:8738; PCOLCE.
DR HPA; ENSG00000106333; Low tissue specificity.
DR MIM; 600270; gene.
DR neXtProt; NX_Q15113; -.
DR OpenTargets; ENSG00000106333; -.
DR PharmGKB; PA33083; -.
DR VEuPathDB; HostDB:ENSG00000106333; -.
DR eggNOG; ENOG502QTZ9; Eukaryota.
DR GeneTree; ENSGT00940000159264; -.
DR HOGENOM; CLU_034096_0_0_1; -.
DR InParanoid; Q15113; -.
DR OMA; WDEHQFC; -.
DR OrthoDB; 862783at2759; -.
DR PhylomeDB; Q15113; -.
DR TreeFam; TF316506; -.
DR PathwayCommons; Q15113; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR SignaLink; Q15113; -.
DR BioGRID-ORCS; 5118; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; PCOLCE; human.
DR EvolutionaryTrace; Q15113; -.
DR GeneWiki; PCOLCE; -.
DR GenomeRNAi; 5118; -.
DR Pharos; Q15113; Tbio.
DR PRO; PR:Q15113; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q15113; protein.
DR Bgee; ENSG00000106333; Expressed in stromal cell of endometrium and 146 other tissues.
DR Genevisible; Q15113; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR GO; GO:0032964; P:collagen biosynthetic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00041; CUB; 2.
DR CDD; cd03576; NTR_PCOLCE; 1.
DR DisProt; DP02622; -.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035814; NTR_PCOLCE.
DR InterPro; IPR028870; PCOLCE.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR45645:SF1; PTHR45645:SF1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00042; CUB; 2.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..449
FT /note="Procollagen C-endopeptidase enhancer 1"
FT /id="PRO_0000022023"
FT DOMAIN 37..149
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 159..273
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 318..437
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 271..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 287..288
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10625689"
FT SITE 288..289
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10625689"
FT SITE 293..294
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10625689"
FT SITE 299..300
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10625689"
FT SITE 303..304
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10625689"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08628"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 90..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 159..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 213..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 318..386
FT /evidence="ECO:0000269|PubMed:12670942"
FT DISULFID 322..389
FT /evidence="ECO:0000269|PubMed:12670942"
FT DISULFID 333..437
FT /evidence="ECO:0000269|PubMed:12670942"
FT STRAND 37..49
FT /evidence="ECO:0007829|PDB:6FZV"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6FZV"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6FZW"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6FZV"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:6FZV"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 336..348
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:1UAP"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1UAP"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1UAP"
FT HELIX 423..434
FT /evidence="ECO:0007829|PDB:1UAP"
SQ SEQUENCE 449 AA; 47972 MW; 3D88430158648796 CRC64;
MLPAATASLL GPLLTACALL PFAQGQTPNY TRPVFLCGGD VKGESGYVAS EGFPNLYPPN
KECIWTITVP EGQTVSLSFR VFDLELHPAC RYDALEVFAG SGTSGQRLGR FCGTFRPAPL
VAPGNQVTLR MTTDEGTGGR GFLLWYSGRA TSGTEHQFCG GRLEKAQGTL TTPNWPESDY
PPGISCSWHI IAPPDQVIAL TFEKFDLEPD TYCRYDSVSV FNGAVSDDSR RLGKFCGDAV
PGSISSEGNE LLVQFVSDLS VTADGFSASY KTLPRGTAKE GQGPGPKRGT EPKVKLPPKS
QPPEKTEESP SAPDAPTCPK QCRRTGTLQS NFCASSLVVT ATVKSMVREP GEGLAVTVSL
IGAYKTGGLD LPSPPTGASL KFYVPCKQCP PMKKGVSYLL MGQVEENRGP VLPPESFVVL
HRPNQDQILT NLSKRKCPSQ PVRAAASQD
