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   27-MAR-2024, entry version 202.
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; 6.
DR   IntAct; Q15113; 24.
DR   MINT; Q15113; -.
DR   STRING; 9606.ENSP00000223061; -.
DR   GlyCosmos; Q15113; 4 sites, 1 glycan.
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; 9606-ENSP00000223061; -.
DR   PeptideAtlas; Q15113; -.
DR   ProteomicsDB; 60442; -.
DR   Antibodypedia; 4318; 286 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   AGR; HGNC:8738; -.
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; 5355450at2759; -.
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 1150 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 148 other cell types or tissues.
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; Spermadhesin, CUB domain; 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; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   PANTHER; PTHR24251:SF24; PROCOLLAGEN C-ENDOPEPTIDASE ENHANCER 1; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00643; C345C; 1.
DR   SMART; SM00042; CUB; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50189; NTR; 1.
DR   Genevisible; Q15113; HS.
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
//