PCOC1_MOUSE
ID PCOC1_MOUSE Reviewed; 468 AA.
AC Q61398; O35113;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Procollagen C-endopeptidase enhancer 1;
DE AltName: Full=P14;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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 NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=CNS;
RX PubMed=2027019; DOI=10.1111/j.1471-4159.1991.tb03476.x;
RA Lecain E., Zelenika D., Laine M.C., Rhyner T., Pessac B.;
RT "Isolation of a novel cDNA corresponding to a transcript expressed in the
RT choroid plexus and leptomeninges.";
RL J. Neurochem. 56:2133-2138(1991).
RN [4]
RP CHARACTERIZATION.
RX PubMed=2689170; DOI=10.1111/j.1432-1033.1989.tb15184.x;
RA Kessler E., Adar R.;
RT "Type I procollagen C-proteinase from mouse fibroblasts. Purification and
RT demonstration of a 55-kDa enhancer glycoprotein.";
RL Eur. J. Biochem. 186:115-121(1989).
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=ICR;
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 [6]
RP GLYCOSYLATION AT ASN-28.
RA Kessler E.;
RL Unpublished observations (JAN-2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH EFEMP2.
RX PubMed=26220971; DOI=10.1093/hmg/ddv308;
RA Papke C.L., Tsunezumi J., Ringuette L.J., Nagaoka H., Terajima M.,
RA Yamashiro Y., Urquhart G., Yamauchi M., Davis E.C., Yanagisawa H.;
RT "Loss of fibulin-4 disrupts collagen synthesis and maturation: implications
RT for pathology resulting from EFEMP2 mutations.";
RL Hum. Mol. Genet. 24:5867-5879(2015).
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:0000269|PubMed:26220971}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in interstitial connective tissues like
CC tendons, calvaria, skin and at a lower level in heart and skeletal
CC muscle. {ECO:0000269|PubMed:2256940}.
CC -!- PTM: Processed from a 55 kDa form to 36 kDa and 34 kDa forms.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40612.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB008548; BAA23280.1; -; mRNA.
DR EMBL; X57337; CAA40612.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39334.1; -.
DR PIR; JH0403; JH0403.
DR RefSeq; NP_032814.2; NM_008788.2.
DR AlphaFoldDB; Q61398; -.
DR SMR; Q61398; -.
DR BioGRID; 202053; 1.
DR STRING; 10090.ENSMUSP00000031731; -.
DR GlyGen; Q61398; 2 sites.
DR iPTMnet; Q61398; -.
DR PhosphoSitePlus; Q61398; -.
DR CPTAC; non-CPTAC-3843; -.
DR MaxQB; Q61398; -.
DR PaxDb; Q61398; -.
DR PRIDE; Q61398; -.
DR ProteomicsDB; 288000; -.
DR Antibodypedia; 4318; 274 antibodies from 33 providers.
DR DNASU; 18542; -.
DR Ensembl; ENSMUST00000031731; ENSMUSP00000031731; ENSMUSG00000029718.
DR GeneID; 18542; -.
DR KEGG; mmu:18542; -.
DR UCSC; uc009adb.1; mouse.
DR CTD; 5118; -.
DR MGI; MGI:105099; Pcolce.
DR VEuPathDB; HostDB:ENSMUSG00000029718; -.
DR eggNOG; ENOG502QTZ9; Eukaryota.
DR GeneTree; ENSGT00940000159264; -.
DR InParanoid; Q61398; -.
DR PhylomeDB; Q61398; -.
DR TreeFam; TF316506; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR BioGRID-ORCS; 18542; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pcolce; mouse.
DR PRO; PR:Q61398; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61398; protein.
DR Bgee; ENSMUSG00000029718; Expressed in vault of skull and 237 other tissues.
DR ExpressionAtlas; Q61398; baseline and differential.
DR Genevisible; Q61398; MM.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0016504; F:peptidase activator activity; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..468
FT /note="Procollagen C-endopeptidase enhancer 1"
FT /id="PRO_0000022024"
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 276..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O08628"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08628"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
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"
FT CONFLICT 178
FT /note="D -> Y (in Ref. 3; CAA40612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 50168 MW; F9B55558147FABAB CRC64;
MLPAALTSFL 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 SALSPGEDVQ RGPQSRSDPK
TGTGPKVKPP TKPKSQPAET PEASPATQAT PVAPAAPSIT CPKQYKRSGT LQSNFCSSSL
VVTGTVKTMV RGPGEGLTVT VSLLGVYKTG GLDLPSPPSG TSLKLYVPCR QMPPMKKGAS
YLLMGQVEEN RGPILPPESF VVLYRSNQDQ ILNNLSKRKC PSQPRTAA
