PCOC2_HUMAN
ID PCOC2_HUMAN Reviewed; 415 AA.
AC Q9UKZ9; B2RCH9; D3DNG4; Q9BRH3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
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; ORFNames=UNQ250/PRO287;
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], AND TISSUE SPECIFICITY.
RX PubMed=10873381; DOI=10.1006/geno.2000.6229;
RA Xu H., Acott T.S., Wirtz M.K.;
RT "Identification and expression of a novel type I procollagen C-proteinase
RT enhancer protein gene from the glaucoma candidate region on 3q21-q24.";
RL Genomics 66:264-273(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Osteoarthritic cartilage;
RX PubMed=11597177; DOI=10.1053/joca.2001.0421;
RA Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J.,
RA Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M., Lark M.W.;
RT "Identification and initial characterization of 5000 expressed sequenced
RT tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA
RT libraries.";
RL Osteoarthritis Cartilage 9:641-653(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 24-38.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, INTERACTION WITH HEPARIN AND TYPE I OR II COLLAGEN, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
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).
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:0000269|PubMed:12393877}.
CC -!- SUBUNIT: Interacts with heparin with high affinity, and type I or II
CC collagen. {ECO:0000269|PubMed:12393877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart, trabecular meshwork,
CC pituitary gland, bladder, mammary gland, trachea and placenta and
CC weakly expressed in the brain. Expressed in cartilage.
CC {ECO:0000269|PubMed:10873381, ECO:0000269|PubMed:11597177,
CC ECO:0000269|PubMed:12393877}.
CC -!- PTM: O-glycosylated; contains sialic acid.
CC {ECO:0000269|PubMed:12393877}.
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; AF098269; AAF04621.1; -; mRNA.
DR EMBL; AY035400; AAK63128.1; -; mRNA.
DR EMBL; AY358557; AAQ88921.1; -; mRNA.
DR EMBL; CR536570; CAG38807.1; -; mRNA.
DR EMBL; AK315121; BAG37576.1; -; mRNA.
DR EMBL; CH471052; EAW78961.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78962.1; -; Genomic_DNA.
DR CCDS; CCDS3127.1; -.
DR RefSeq; NP_037495.1; NM_013363.3.
DR AlphaFoldDB; Q9UKZ9; -.
DR SMR; Q9UKZ9; -.
DR BioGRID; 117746; 28.
DR IntAct; Q9UKZ9; 9.
DR STRING; 9606.ENSP00000295992; -.
DR GlyGen; Q9UKZ9; 2 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q9UKZ9; -.
DR PhosphoSitePlus; Q9UKZ9; -.
DR BioMuta; PCOLCE2; -.
DR DMDM; 67470587; -.
DR jPOST; Q9UKZ9; -.
DR MassIVE; Q9UKZ9; -.
DR MaxQB; Q9UKZ9; -.
DR PaxDb; Q9UKZ9; -.
DR PeptideAtlas; Q9UKZ9; -.
DR PRIDE; Q9UKZ9; -.
DR ProteomicsDB; 84920; -.
DR Antibodypedia; 2145; 159 antibodies from 23 providers.
DR DNASU; 26577; -.
DR Ensembl; ENST00000295992.8; ENSP00000295992.3; ENSG00000163710.9.
DR GeneID; 26577; -.
DR KEGG; hsa:26577; -.
DR MANE-Select; ENST00000295992.8; ENSP00000295992.3; NM_013363.4; NP_037495.1.
DR UCSC; uc003evd.4; human.
DR CTD; 26577; -.
DR DisGeNET; 26577; -.
DR GeneCards; PCOLCE2; -.
DR HGNC; HGNC:8739; PCOLCE2.
DR HPA; ENSG00000163710; Tissue enhanced (adipose tissue, heart muscle).
DR MIM; 607064; gene.
DR neXtProt; NX_Q9UKZ9; -.
DR OpenTargets; ENSG00000163710; -.
DR PharmGKB; PA33084; -.
DR VEuPathDB; HostDB:ENSG00000163710; -.
DR eggNOG; ENOG502QRMG; Eukaryota.
DR GeneTree; ENSGT00940000157649; -.
DR HOGENOM; CLU_034096_0_0_1; -.
DR InParanoid; Q9UKZ9; -.
DR OMA; IFCAWTL; -.
DR OrthoDB; 862783at2759; -.
DR PhylomeDB; Q9UKZ9; -.
DR TreeFam; TF316506; -.
DR PathwayCommons; Q9UKZ9; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; Q9UKZ9; -.
DR BioGRID-ORCS; 26577; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; PCOLCE2; human.
DR GeneWiki; PCOLCE2; -.
DR GenomeRNAi; 26577; -.
DR Pharos; Q9UKZ9; Tbio.
DR PRO; PR:Q9UKZ9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UKZ9; protein.
DR Bgee; ENSG00000163710; Expressed in calcaneal tendon and 171 other tissues.
DR ExpressionAtlas; Q9UKZ9; baseline and differential.
DR Genevisible; Q9UKZ9; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..415
FT /note="Procollagen C-endopeptidase enhancer 2"
FT /id="PRO_0000022020"
FT DOMAIN 33..144
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 154..268
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 297..415
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 86..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 154..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 208..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 297..364
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT DISULFID 301..367
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT DISULFID 312..415
FT /evidence="ECO:0000250|UniProtKB:Q15113"
FT VARIANT 280
FT /note="V -> A (in dbSNP:rs35692900)"
FT /id="VAR_051264"
FT VARIANT 292
FT /note="P -> T (in dbSNP:rs17554211)"
FT /id="VAR_022448"
SQ SEQUENCE 415 AA; 45717 MW; B9AA87FD9AAF7A5B CRC64;
MRGANAWAPL CLLLAAATQL SRQQSPERPV FTCGGILTGE SGFIGSEGFP GVYPPNSKCT
WKITVPEGKV VVLNFRFIDL ESDNLCRYDF VDVYNGHANG QRIGRFCGTF RPGALVSSGN
KMMVQMISDA NTAGNGFMAM FSAAEPNERG DQYCGGLLDR PSGSFKTPNW PDRDYPAGVT
CVWHIVAPKN QLIELKFEKF DVERDNYCRY DYVAVFNGGE VNDARRIGKY CGDSPPAPIV
SERNELLIQF LSDLSLTADG FIGHYIFRPK KLPTTTEQPV TTTFPVTTGL KPTVALCQQK
CRRTGTLEGN YCSSDFVLAG TVITTITRDG SLHATVSIIN IYKEGNLAIQ QAGKNMSARL
TVVCKQCPLL RRGLNYIIMG QVGEDGRGKI MPNSFIMMFK TKNQKLLDAL KNKQC