PCOC1_RAT
ID PCOC1_RAT Reviewed; 468 AA.
AC O08628;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=9303490; DOI=10.1002/hep.510260312;
RA Ogata I., Auster A.S., Matsui A., Greenwel P., Geerts A., D'Amico T.,
RA Fujiwara K., Kessler E., Rojkind M.;
RT "Up-regulation of type I procollagen C-proteinase enhancer protein
RT messenger RNA in rats with CCl4-induced liver fibrosis.";
RL Hepatology 26:611-617(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Aorta;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Fischer 344;
RA Masuda M., Igarashi H., Kano M., Yoshikura H.;
RT "Proviral integration into the procollagen C-proteinase enhancer protein
RT gene and its effects in cultured rat fibroblasts revealed by an excisable
RT 'hit-and-run' retroviral vector.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=2256940; DOI=10.1016/s0006-291x(05)81024-1;
RA Kessler E., Mould A.P., Hulmes D.J.S.;
RT "Procollagen type I C-proteinase enhancer is a naturally occurring
RT connective tissue glycoprotein.";
RL Biochem. Biophys. Res. Commun. 173:81-86(1990).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41 AND SER-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Binds to the C-terminal propeptide of type I procollagen and
CC enhances procollagen C-proteinase activity.
CC -!- SUBUNIT: Interacts with EFEMP2. {ECO:0000250|UniProtKB:Q61398}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in collagen-rich
CC tissues, especially tendon. Also expressed in cornea and sterna.
CC {ECO:0000269|PubMed:2256940}.
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DR EMBL; U94710; AAB93478.1; -; mRNA.
DR EMBL; AB008534; BAA23217.1; -; mRNA.
DR EMBL; AF016503; AAD01592.1; -; mRNA.
DR EMBL; AF016506; AAD01598.1; -; Genomic_DNA.
DR RefSeq; NP_062110.1; NM_019237.1.
DR AlphaFoldDB; O08628; -.
DR SMR; O08628; -.
DR STRING; 10116.ENSRNOP00000001887; -.
DR GlyGen; O08628; 2 sites.
DR iPTMnet; O08628; -.
DR PhosphoSitePlus; O08628; -.
DR PaxDb; O08628; -.
DR PRIDE; O08628; -.
DR GeneID; 29569; -.
DR KEGG; rno:29569; -.
DR UCSC; RGD:3270; rat.
DR CTD; 5118; -.
DR RGD; 3270; Pcolce.
DR VEuPathDB; HostDB:ENSRNOG00000025001; -.
DR eggNOG; ENOG502QTZ9; Eukaryota.
DR InParanoid; O08628; -.
DR OrthoDB; 862783at2759; -.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-2243919; Crosslinking of collagen fibrils.
DR PRO; PR:O08628; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000025001; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; O08628; baseline and differential.
DR Genevisible; O08628; RN.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0016504; F:peptidase activator activity; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR CDD; cd00041; CUB; 2.
DR CDD; cd03576; NTR_PCOLCE; 1.
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 Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..468
FT /note="Procollagen C-endopeptidase enhancer 1"
FT /id="PRO_0000022025"
FT DOMAIN 36..148
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 158..272
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 341..460
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 271..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 89..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 158..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 212..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 341..409
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT DISULFID 356..460
FT /evidence="ECO:0000250|UniProtKB:Q15113"
SQ SEQUENCE 468 AA; 50185 MW; B4AA1C151323969B CRC64;
MLPAALTSLL GPFLLAWVLP LARGQTPNYT RPVFLCGGDV TGESGYVASE GFPNLYPPNK
KCIWTITVPE GQTVSLSFRV FDMELHPSCR YDALEVFAGS GTSGQRLGRF CGTFRPAPVV
APGNQVTLRM TTDEGTGGRG FLLWYSGRAT SGTEHQFCGG RMEKAQGTLT TPNWPESDYP
PGISCSWHII APSNQVIMLT FGKFDVEPDT YCRYDSVSVF NGAVSDDSKR LGKFCGDKAP
SPISSEGNEL LVQFVSDLSV TADGFSASYR TLPRDAVEKE SAPSPGEDAQ HGPQSRSDPK
TGTGPKVKPP SKPKVQPVEK PEGSPATQAT PVAPDAPSIT CPKQYKRSGT LQSNFCSSSL
VVTGTVKAMV RGPGEGLTVT VSLLGVYKTG DLDLPSPASG TSLKFYVPCK QMPPMKKGAS
YLLMGQVEEN RGPILPPESF VVLYRPNQDQ ILSNLSKRKC PSQPRPDA
