PCOC2_MOUSE
ID PCOC2_MOUSE Reviewed; 414 AA.
AC Q8R4W6; Q3V1K6; Q9CX06;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Procollagen C-endopeptidase enhancer 2;
DE AltName: Full=Procollagen COOH-terminal proteinase enhancer 2;
DE Short=PCPE-2;
DE Short=Procollagen C-proteinase enhancer 2;
DE Flags: Precursor;
GN Name=Pcolce2; Synonyms=Pcpe2;
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 DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=12393877; DOI=10.1074/jbc.m209891200;
RA Steiglitz B.M., Keene D.R., Greenspan D.S.;
RT "PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2)
RT that is a collagen-binding protein differing in distribution of expression
RT and post-translational modification from the previously described PCPE1.";
RL J. Biol. Chem. 277:49820-49830(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
CC -!- FUNCTION: Binds to the C-terminal propeptide of types I and II
CC procollagens and may enhance the cleavage of that propeptide by BMP1.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with heparin with high affinity, and type I or II
CC collagen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development, with
CC expression level decreasing from 7 to 11 dpc and more abundant levels
CC of expression at 15 and 17 dpc. First detectable at relatively low
CC level at 10.5 dpc in the area of the third and fourth branchial arches.
CC At 13.5 dpc easily discernible expression seems primarily confined to
CC the cartilage primordia of future bones. At 15.5 dpc expressed at the
CC highest levels in skeletal elements in the interior non-ossified
CC regions of cartilaginous structures and excluded from regions of
CC ossification. {ECO:0000269|PubMed:12393877}.
CC -!- PTM: O-glycosylated; contains sialic acid. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF352788; AAL83947.1; -; mRNA.
DR EMBL; AK010249; BAB26794.1; -; mRNA.
DR EMBL; AK132395; BAE21144.1; -; mRNA.
DR EMBL; BC051174; AAH51174.1; -; mRNA.
DR CCDS; CCDS23410.1; -.
DR RefSeq; NP_083896.1; NM_029620.2.
DR AlphaFoldDB; Q8R4W6; -.
DR SMR; Q8R4W6; -.
DR STRING; 10090.ENSMUSP00000015498; -.
DR GlyGen; Q8R4W6; 1 site.
DR PhosphoSitePlus; Q8R4W6; -.
DR MaxQB; Q8R4W6; -.
DR PaxDb; Q8R4W6; -.
DR PeptideAtlas; Q8R4W6; -.
DR PRIDE; Q8R4W6; -.
DR ProteomicsDB; 288077; -.
DR Antibodypedia; 2145; 159 antibodies from 23 providers.
DR DNASU; 76477; -.
DR Ensembl; ENSMUST00000015498; ENSMUSP00000015498; ENSMUSG00000015354.
DR GeneID; 76477; -.
DR KEGG; mmu:76477; -.
DR UCSC; uc009rbg.1; mouse.
DR CTD; 26577; -.
DR MGI; MGI:1923727; Pcolce2.
DR VEuPathDB; HostDB:ENSMUSG00000015354; -.
DR eggNOG; ENOG502QRMG; Eukaryota.
DR GeneTree; ENSGT00940000157649; -.
DR HOGENOM; CLU_034096_0_0_1; -.
DR InParanoid; Q8R4W6; -.
DR OMA; IFCAWTL; -.
DR OrthoDB; 862783at2759; -.
DR PhylomeDB; Q8R4W6; -.
DR TreeFam; TF316506; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 76477; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Pcolce2; mouse.
DR PRO; PR:Q8R4W6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R4W6; protein.
DR Bgee; ENSMUSG00000015354; Expressed in humerus cartilage element and 195 other tissues.
DR Genevisible; Q8R4W6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR008993; TIMP-like_OB-fold.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..414
FT /note="Procollagen C-endopeptidase enhancer 2"
FT /id="PRO_0000022021"
FT DOMAIN 32..143
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 153..267
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 296..414
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 85..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 153..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 207..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 296..363
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT DISULFID 300..366
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT DISULFID 311..414
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT CONFLICT 167
FT /note="P -> S (in Ref. 1; AAL83947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45408 MW; E51A29A352A2CF1D CRC64;
MGGASACIPL CLLLATARMA RPQTPERPVF TCGGILTGES GFIGSEGFPG MYPPNSKCTW
KITVPEGKVV VLNFRFIDLE NDNLCRYDFV DVYNGHANGQ RIGRFCGTFR PGSLVASGNK
MTVQMISDAN TAGSGFMATY SAAAPDGKGD RYCGGRLEKP SGTFKTPNWP DRDYPVGVTC
VWHIIAPKNQ LIELKFEKFD VERDNYCRYD YVAVFNGGEV NDAKRIGKYC GDSPPVPIVS
ERNELLIQFL SDLSLTADGF IGHYKFRPKK FPTTTTTPVT TTLPVTTGLK PTVALCQQKC
RRMGTLESNY CSSNFVLAGT VITTVTRGGS LHATVSIISI YREGNLAIQQ AGKNMSVKLT
VVCRQCPLLR RGLNYIIMGQ VGEDGRGKIM PNSFVKMFKN KNQKPMNALK NKQC
