EPYC_MOUSE
ID EPYC_MOUSE Reviewed; 322 AA.
AC P70186;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Epiphycan;
DE AltName: Full=Dermatan sulfate proteoglycan 3;
DE AltName: Full=Proteoglycan-Lb;
DE Short=PG-Lb;
DE AltName: Full=Small chondroitin/dermatan sulfate proteoglycan;
DE Flags: Precursor;
GN Name=Epyc; Synonyms=Dspg3, Pglb;
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 TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Epiphyseal cartilage;
RX PubMed=8836137; DOI=10.1042/bj3180909;
RA Kurita K., Shinomura T., Ujita M., Zako M., Kida D., Iwata H., Kimata K.;
RT "Occurrence of PG-Lb, a leucine-rich small chondroitin/dermatan sulphate
RT proteoglycan in mammalian epiphyseal cartilage: molecular cloning and
RT sequence analysis of the mouse cDNA.";
RL Biochem. J. 318:909-914(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RC STRAIN=129/Sv;
RX PubMed=9560328; DOI=10.1042/bj3310959;
RA Iwata Y., Shinomura T., Kurita K., Zako M., Kimata K.;
RT "The gene structure and organization of mouse PG-Lb, a small
RT chondroitin/dermatan sulphate proteoglycan.";
RL Biochem. J. 331:959-964(1998).
RN [5]
RP EXPRESSION DURING DEVELOPMENT.
RX PubMed=10633869;
RX DOI=10.1002/(sici)1097-0177(199912)216:4/5<499::aid-dvdy18>3.0.co;2-s;
RA Johnson H.J., Shinomura T., Eberspaecher H., Pinero G., Decrombrugghe B.,
RA Hoeoek M.;
RT "Expression and localization of PG-Lb/epiphycan during mouse development.";
RL Dev. Dyn. 216:499-510(1999).
CC -!- FUNCTION: May have a role in bone formation and also in establishing
CC the ordered structure of cartilage through matrix organization.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Note=Surrounding resting, proliferating, and hypertrophic
CC chondrocytes.
CC -!- TISSUE SPECIFICITY: Confined to the middle zone of embryonic epiphyseal
CC cartilage consisting of flattened chondrocytes and the ossifying region
CC in the limb buds of chick embryos. Has also been detected in testis.
CC {ECO:0000269|PubMed:8836137}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 12.5 dpc and is restricted to
CC developing cartilage.
CC -!- PTM: The O-linked polysaccharide on Ser-96 is probably the mucin type
CC linked to GalNAc. There is one glycosaminoglycan chain, known to be
CC dermatan sulfate, and it is probably the O-glycosylation at Ser-64 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class III subfamily. {ECO:0000305}.
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DR EMBL; D78274; BAA11337.1; -; mRNA.
DR EMBL; D87187; BAA28770.1; -; Genomic_DNA.
DR EMBL; BC012695; AAH12695.1; -; mRNA.
DR EMBL; AK015223; BAB29756.1; -; mRNA.
DR CCDS; CCDS24143.1; -.
DR PIR; S72271; S72271.
DR RefSeq; NP_031910.1; NM_007884.2.
DR AlphaFoldDB; P70186; -.
DR SMR; P70186; -.
DR STRING; 10090.ENSMUSP00000100922; -.
DR GlyGen; P70186; 4 sites.
DR iPTMnet; P70186; -.
DR PhosphoSitePlus; P70186; -.
DR PaxDb; P70186; -.
DR PRIDE; P70186; -.
DR ProteomicsDB; 275875; -.
DR Antibodypedia; 29993; 128 antibodies from 23 providers.
DR Ensembl; ENSMUST00000020094; ENSMUSP00000020094; ENSMUSG00000019936.
DR Ensembl; ENSMUST00000105285; ENSMUSP00000100922; ENSMUSG00000019936.
DR GeneID; 13516; -.
DR KEGG; mmu:13516; -.
DR UCSC; uc007gxb.1; mouse.
DR CTD; 1833; -.
DR MGI; MGI:107942; Epyc.
DR VEuPathDB; HostDB:ENSMUSG00000019936; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157574; -.
DR HOGENOM; CLU_067583_0_0_1; -.
DR InParanoid; P70186; -.
DR OMA; CLLCTCM; -.
DR OrthoDB; 1109019at2759; -.
DR PhylomeDB; P70186; -.
DR TreeFam; TF351924; -.
DR BioGRID-ORCS; 13516; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Epyc; mouse.
DR PRO; PR:P70186; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P70186; protein.
DR Bgee; ENSMUSG00000019936; Expressed in epithelium of cochlear duct and 118 other tissues.
DR Genevisible; P70186; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0061975; P:articular cartilage development; IGI:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR027217; Epiphycan.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR043547; Mimecan/Epiphycan.
DR PANTHER; PTHR46269; PTHR46269; 1.
DR PANTHER; PTHR46269:SF3; PTHR46269:SF3; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 4.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..322
FT /note="Epiphycan"
FT /id="PRO_0000032769"
FT DOMAIN 106..143
FT /note="LRRNT"
FT REPEAT 144..165
FT /note="LRR 1"
FT REPEAT 168..189
FT /note="LRR 2"
FT REPEAT 192..213
FT /note="LRR 3"
FT REPEAT 238..258
FT /note="LRR 4"
FT REPEAT 259..280
FT /note="LRR 5"
FT REPEAT 290..310
FT /note="LRR 6"
FT REGION 58..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 64
FT /note="O-linked (Xyl...) (dermatan sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..130
FT /evidence="ECO:0000250"
FT DISULFID 279..312
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 36763 MW; C9C8CBEBECDAC19A CRC64;
MGMLARVALG LIIIDAVLAA PTTELFNYDS EVYDAILEDT GTFYNYEHIP DNHVENEKVS
ERLSGNRELL TPGPQLGDNQ DEDKDEESTP RLIDGSSPQE PEFPGLLGPH TNEDFPTCLL
CTCISTTVYC DDHELDAIPP LPKKTTYFYS RFNRIKKINK NDFASLNDLK RIDLTSNLIS
EIDEDAFRKL PHLQELVLRD NKIKQLPELP NTLTFIDISN NRLGRKGIKQ EAFKDMYDLH
HLYITDNSLD HIPLPLPESL RALHLQNNDI LEMHEDTFCN VKNLTYVRKA LEDIRLDGNP
INLSRTPQAY MCLPRLPIGS FI
