CILP1_MOUSE
ID CILP1_MOUSE Reviewed; 1184 AA.
AC Q66K08; Q7TSS0; Q7TSS1; Q8BV01;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Cartilage intermediate layer protein 1;
DE Short=CILP-1;
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 1 C1;
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 1 C2;
DE Flags: Precursor;
GN Name=Cilp;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51 AND 344-1184.
RC STRAIN=129/SvJ;
RA Lorenzo P., Heinegaard D.;
RT "The mouse Cilp gene.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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: Probably plays a role in cartilage scaffolding. May act by
CC antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to
CC suppress IGF1-induced proliferation and sulfated proteoglycan
CC synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May
CC inhibit TGFB1-mediated induction of cartilage matrix genes via its
CC interaction with TGFB1. Overexpression may lead to impair chondrocyte
CC growth and matrix repair and indirectly promote inorganic pyrophosphate
CC (PPi) supersaturation in aging and osteoarthritis cartilage (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with TGFB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in articular and meniscal cartilage (at
CC protein level). Primarily localizes to the superficial and intermediate
CC zones of articular cartilage (at protein level).
CC {ECO:0000269|PubMed:21880736}.
CC -!- DEVELOPMENTAL STAGE: Detected in articular cartilage from 8 weeks of
CC age, but not at earlier stages (at protein level).
CC {ECO:0000269|PubMed:21880736}.
CC -!- PTM: Cleaved into 2 chains possibly by a furin-like protease upon or
CC preceding secretion. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38252.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK081544; BAC38252.1; ALT_FRAME; mRNA.
DR EMBL; BC080666; AAH80666.1; -; mRNA.
DR EMBL; AY116589; AAM92571.1; -; Genomic_DNA.
DR EMBL; AY116591; AAM92572.1; -; Genomic_DNA.
DR EMBL; AY116590; AAM92572.1; JOINED; Genomic_DNA.
DR RefSeq; NP_775561.1; NM_173385.2.
DR AlphaFoldDB; Q66K08; -.
DR BioGRID; 229526; 4.
DR STRING; 10090.ENSMUSP00000036631; -.
DR GlyGen; Q66K08; 8 sites.
DR iPTMnet; Q66K08; -.
DR PhosphoSitePlus; Q66K08; -.
DR MaxQB; Q66K08; -.
DR PaxDb; Q66K08; -.
DR PeptideAtlas; Q66K08; -.
DR PRIDE; Q66K08; -.
DR ProteomicsDB; 283841; -.
DR GeneID; 214425; -.
DR KEGG; mmu:214425; -.
DR UCSC; uc009qcz.1; mouse.
DR CTD; 8483; -.
DR MGI; MGI:2444507; Cilp.
DR eggNOG; ENOG502QQ8H; Eukaryota.
DR InParanoid; Q66K08; -.
DR OrthoDB; 629181at2759; -.
DR PhylomeDB; Q66K08; -.
DR TreeFam; TF330132; -.
DR Reactome; R-MMU-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
DR BioGRID-ORCS; 214425; 6 hits in 71 CRISPR screens.
DR PRO; PR:Q66K08; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q66K08; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:MGI.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
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; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1184
FT /note="Cartilage intermediate layer protein 1"
FT /id="PRO_0000014674"
FT CHAIN 22..?724
FT /note="Cartilage intermediate layer protein 1 C1"
FT /id="PRO_0000014675"
FT CHAIN ?725..1184
FT /note="Cartilage intermediate layer protein 1 C2"
FT /id="PRO_0000014676"
FT DOMAIN 150..201
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 309..393
FT /note="Ig-like C2-type"
FT REGION 1138..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1056
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..195
FT /evidence="ECO:0000250"
FT DISULFID 165..200
FT /evidence="ECO:0000250"
FT DISULFID 177..185
FT /evidence="ECO:0000250"
FT DISULFID 330..376
FT /evidence="ECO:0000250"
FT CONFLICT 499
FT /note="T -> A (in Ref. 1; BAC38252 and 3; AAM92572)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="M -> L (in Ref. 3; AAM92572)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="Q -> E (in Ref. 3; AAM92572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1184 AA; 132334 MW; C83B97AC0D0DC9D3 CRC64;
MAAIKTWVFS FLVLEVTTVL GRQTMLAQSV RRVQPVKRTP KTLAKPADSQ ESPGEWTTWF
NIDHPGGQGD YERLDAIRFY YGERVCARPL RLEARTTDWM PAGSTGQVVH GSPREGFWCL
NREQRPGQNC SNYTVRFLCP PGSLRGDAEH IWSSWSPWSK CSAACGHTGV QTRTRTCLAQ
TVSLCSEATE EGQLCMSQAC TACDLTCPMG QVNADCDACM CQDFMLHGAI SLPGGGPAPG
AAVYLLAKAP KMLTRTDSSG RFRVPGLCPD GKTILKITKT KFAPIMITMP KTSLKSATIN
AEFVRAETPY IVMNPEMKAR RAGQSVSLCC KATGKPSPDK YFWYHNNTLL DPSLYKHESK
LVLRNLQQDQ AGEYFCKAQS DAGAVKSKVT QLTVIAHDET PCNPTPESYL IRLPHDCFQN
ASNSFYYDVG RCPIKTCAGQ QDNGIRCRDA VENCCGISRT EEREIQCSGY TLPTKVAVEC
SCQRCAETRS IVRGRVTATD NGEPMRFGHV YMGNNRVSMT GYKGTFTLHI PQDTERLVLT
FVDRLQKFVN TTKVLPFNKK GSAVFHEIKM LRQKEPITLE AMETNIIPLG EVIGEDPVAE
LEIPSKSFYR QNGEPFTGKV KASVTFLDPR NISTATAAQS DLNFINDEGD TFPLRTYGMF
SVDFRDEATS ESLNAGKVKV HLDSTQVKMP EHVPAMKLWS LNPDTGLWEE EGDFKFESQR
RNKREERTFL VGNMEIRERR LFNLDVPESR RCFIKVRTYR SERFLPSEQI QGVVVSVINL
EPRTGFSSNP RAWGRFDSVI TGPNGACLPA FCDDQSPDAY SVYVLASLSG EELEAVESSP
KFNPNAIGVP QPYLNKLKYR RTDHEDPRVK KTAFQISMAK PRPNSAEESN GPIYAFENLR
ACEEAPPSAA HFRFYQIEGD RYDYNTVPFN EDDPMSWTED YLAWWPKPME FRACYIKVKI
VGPLEVNVRS RNMGGTHRQT VGKLYGIRDV KSTRDRDQPN VSSACLEFKC SGMLYDQDRV
DRTLVKVIPQ GSCHRASVNS MLHEYLVNHL PLAVNNDTSE YTMLAPLDPL GHNYGIYTVT
DQDPRTAKEI ALGRCFDGTS DGSSRIMKSN VGVALTFNCA ERQVGRQSAF QYLQSTPARS
PATGTVQGRV PAMRQQRASR GGLRRRGSMA PLRFSGVAQQ PLSN
