CILP2_MOUSE
ID CILP2_MOUSE Reviewed; 1162 AA.
AC D3Z7H8;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cartilage intermediate layer protein 2 {ECO:0000312|MGI:MGI:1915959};
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 2 C1 {ECO:0000250|UniProtKB:O75339};
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 2 C2 {ECO:0000250|UniProtKB:O75339};
DE Flags: Precursor;
GN Name=Cilp2 {ECO:0000312|MGI:MGI:1915959};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=21880736; DOI=10.1074/jbc.m111.248039;
RA Bernardo B.C., Belluoccio D., Rowley L., Little C.B., Hansen U.,
RA Bateman J.F.;
RT "Cartilage intermediate layer protein 2 (CILP-2) is expressed in articular
RT and meniscal cartilage and down-regulated in experimental osteoarthritis.";
RL J. Biol. Chem. 286:37758-37767(2011).
CC -!- FUNCTION: May play a role in cartilage scaffolding.
CC {ECO:0000250|UniProtKB:O75339}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q8IUL8}.
CC -!- TISSUE SPECIFICITY: Expressed in articulated and meniscal cartilage (at
CC protein level). Also detected in heart, skeletal muscle and brain. Not
CC detected in growth plate cartilage. {ECO:0000269|PubMed:21880736}.
CC -!- DEVELOPMENTAL STAGE: In the knee joint, detected in articular cartilage
CC from 2 weeks of age but not at earlier stages (at protein level).
CC Initially localizes to the surface zone of articular cartilage but by
CC maturity (8 weeks) is found in the intermediate to deep zones (at
CC protein level). {ECO:0000269|PubMed:21880736}.
CC -!- PTM: May be cleaved into 2 chains possibly by a furin-like protease
CC upon or preceding secretion. {ECO:0000305|PubMed:21880736}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21880736}.
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DR EMBL; AC158564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40363.1; -.
DR RefSeq; NP_081094.2; NM_026818.2.
DR AlphaFoldDB; D3Z7H8; -.
DR STRING; 10090.ENSMUSP00000061544; -.
DR GlyGen; D3Z7H8; 1 site.
DR iPTMnet; D3Z7H8; -.
DR PhosphoSitePlus; D3Z7H8; -.
DR EPD; D3Z7H8; -.
DR MaxQB; D3Z7H8; -.
DR PaxDb; D3Z7H8; -.
DR PRIDE; D3Z7H8; -.
DR ProteomicsDB; 283558; -.
DR Antibodypedia; 48010; 82 antibodies from 19 providers.
DR Ensembl; ENSMUST00000057831; ENSMUSP00000061544; ENSMUSG00000044006.
DR GeneID; 68709; -.
DR KEGG; mmu:68709; -.
DR UCSC; uc009lyb.2; mouse.
DR CTD; 148113; -.
DR MGI; MGI:1915959; Cilp2.
DR VEuPathDB; HostDB:ENSMUSG00000044006; -.
DR eggNOG; ENOG502QQ8H; Eukaryota.
DR GeneTree; ENSGT00390000008152; -.
DR HOGENOM; CLU_008073_0_0_1; -.
DR InParanoid; D3Z7H8; -.
DR OMA; PPVQSYW; -.
DR OrthoDB; 629181at2759; -.
DR PhylomeDB; D3Z7H8; -.
DR TreeFam; TF330132; -.
DR BioGRID-ORCS; 68709; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cilp2; mouse.
DR PRO; PR:D3Z7H8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; D3Z7H8; protein.
DR Bgee; ENSMUSG00000044006; Expressed in skin of snout and 89 other tissues.
DR Genevisible; D3Z7H8; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR039675; CILP1/CILP2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR025155; WxxW_domain.
DR PANTHER; PTHR15031; PTHR15031; 1.
DR Pfam; PF13330; Mucin2_WxxW; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Immunoglobulin domain; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1162
FT /note="Cartilage intermediate layer protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003052865"
FT CHAIN 22..?715
FT /note="Cartilage intermediate layer protein 2 C1"
FT /evidence="ECO:0000250|UniProtKB:O75339"
FT /id="PRO_0000437175"
FT CHAIN ?716..1162
FT /note="Cartilage intermediate layer protein 2 C2"
FT /evidence="ECO:0000250|UniProtKB:O75339"
FT /id="PRO_0000437176"
FT DOMAIN 146..197
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 293..377
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 23..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 162..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 173..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 314..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1162 AA; 125934 MW; 96C290391AB60A37 CRC64;
MASPLPLLYL CLAALHLAGA RDATPTEEHT STARGLQGRP PDTGQPSPAL EDWEEASEWT
SWFNVDHPGG DGDFESLAAI RFYYGPARVC PRPLALEART TDWALPAAMG ERVHANPERG
FWCLNREQPR GRRCSNYHVR FRCPLEAAWG AWGAWGLCSK SCGLGRRLRR RSCQSSSGDT
CPGSPQEAQK CVRSRCPGCS SDTCGCPNHI LLGSVVTPSG RPLSGARVSL RTRPGTIATS
GTHGTFQVPG VCAGSKASVS AQMNGFSAGT AQAHANSSNT ATVTIILEEL GKPYLVKHPE
SRVREAGQNV TFCCKASGTP MPKKYSWFHN GTLLDRRQQG SGPHLELQGL HQAQAGEYHC
KAWNEAGTVR SRAALLTILA PGQQACDPRP QEHLIKLPDD CGQPGGGPTY LDVGLCADTR
CPGPVGSGPR CGDAGSRCCS VLRLESRDIR CSGYVLPVKV VAECGCRKCL PRRGLVRGRV
VAADSGEPLR FARILLGRAP IGFTSYQGDF TIEVPPATER LVVTFVDPSG DFVDSVRVLP
FDPRGAGVYH EIRALRKAAA VLLDAERGGE IPLGSTEEAP ALGELVLPPG TFHHPDGRPY
TGPVEARVTF VDPRDLASAS AASSDLRFLD SAGELAPLRT YGMFAVDLRA PGSTEQLHVA
RADVHVDADH VRMPGHAEAL ALWSLDPETG LWEEEGSEQG SGGFRRETAA ARVRREERAF
LVGALTMRER RLFNLDVPER RRCFVKVRAY GTDRFAPAEQ VQGVVVTLLN LEPAPGFTAN
PRAWGRFDSA VTGPNGACVP AFCDAEKPDA YTAFVTAALG GEELEAAPSR PRATAAVVGV
AQPYLERLGY QRTDHDDPAL KRTGFRLNLA RPRAGHESEA HGPVYPWRRL RDCEDAPVTD
SHFRFSRVEA DKYEYDVVPF HEGAPASWTG DLLAWWPNPQ EFRACFLKVR LQGPQEYMVR
SHNAGGTHEA TRGRLYGLRD TRSVRHPERP GASAACVEFK CGGMLFDQRQ VDRTLVTVTP
QGSCRRVAVN TLLQDYLARH PPLAAADDPA AFAMLAPLDA LGHNYGVYTV TDQSPRLAKE
IAIGRCFDGS SDGFSREMKA DAGTAVTFQC REPPARPSLF QRLLENPSSA LGDIRREMGQ
ATRYSRVNQT QAGDTGPFGP GQ
