CILP1_PIG
ID CILP1_PIG Reviewed; 599 AA.
AC O19112; Q9TS02;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Cartilage intermediate layer protein 1;
DE Short=CILP-1;
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 1 C2;
DE Flags: Fragment;
GN Name=CILP; Synonyms=NTPPH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9332376; DOI=10.1016/s0378-1119(97)00272-2;
RA Masuda I., Halligan B.D., Barbieri J.T., Haas A.L., Ryan L.M.,
RA McCarty D.J.;
RT "Molecular cloning and expression of a porcine chondrocyte nucleotide
RT pyrophosphohydrolase.";
RL Gene 197:277-287(1997).
RN [2]
RP PROTEIN SEQUENCE OF 141-167.
RX PubMed=7860751; DOI=10.1172/jci117716;
RA Masuda I., Hamada J., Haas A.L., Ryan L.M., McCarty D.J.;
RT "A unique ectonucleotide pyrophosphohydrolase associated with porcine
RT chondrocyte-derived vesicles.";
RL J. Clin. Invest. 95:699-704(1995).
RN [3]
RP ERRATUM OF PUBMED:7860751.
RX PubMed=7635956; DOI=10.1172/jci117716c1;
RA Masuda I., Hamada J., Haas A.L., Ryan L.M., McCarty D.J.;
RL J. Clin. Invest. 96:1179-1179(1995).
RN [4]
RP INDUCTION.
RX PubMed=11145028;
RX DOI=10.1002/1529-0131(200012)43:12<2703::aid-anr10>3.0.co;2-y;
RA Hirose J., Masuda I., Ryan L.M.;
RT "Expression of cartilage intermediate layer protein/nucleotide
RT pyrophosphohydrolase parallels the production of extracellular inorganic
RT pyrophosphate in response to growth factors and with aging.";
RL Arthritis Rheum. 43:2703-2711(2000).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=11341331; DOI=10.1359/jbmr.2001.16.5.868;
RA Masuda I., Iyama K., Halligan B.D., Barbieri J.T., Haas A.L., McCarty D.J.,
RA Ryan L.M.;
RT "Variations in site and levels of expression of chondrocyte nucleotide
RT pyrophosphohydrolase with aging.";
RL J. Bone Miner. Res. 16:868-875(2001).
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: Specifically expressed in cartilage. Expressed at
CC lower level in young cartilage than in adult cartilage. In adult
CC cartilage, it is highly expressed throughout middeep zones.
CC -!- INDUCTION: Up-regulated upon TGFB1 treatment, and down-regulated by
CC IGF1. {ECO:0000269|PubMed:11145028}.
CC -!- PTM: Cleaved into 2 chains possibly by a furin-like protease upon or
CC preceding secretion. {ECO:0000250}.
CC -!- CAUTION: Was originally (PubMed:9332376 and PubMed:7860751) thought to
CC constitute the ATP pyrophosphatase enzyme (NTPPH). However, it was
CC later shown that it is probably not the case. {ECO:0000305}.
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; U83114; AAC48770.1; -; mRNA.
DR AlphaFoldDB; O19112; -.
DR STRING; 9823.ENSSSCP00000005303; -.
DR PaxDb; O19112; -.
DR PeptideAtlas; O19112; -.
DR PRIDE; O19112; -.
DR eggNOG; ENOG502QQ8H; Eukaryota.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IBA:GO_Central.
DR InterPro; IPR039675; CILP1/CILP2.
DR PANTHER; PTHR15031; PTHR15031; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Extracellular matrix; Glycoprotein;
KW Reference proteome; Secreted.
FT CHAIN <1..599
FT /note="Cartilage intermediate layer protein 1 C2"
FT /id="PRO_0000014677"
FT REGION 550..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 154..155
FT /note="ER -> RT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="ES -> AT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 599 AA; 67433 MW; CCC4D08BCB1CF2D1 CRC64;
QHYPLGDMDG EDPMGELEIP SKSFYRQNGE PYTGKVKASV TFLDPRNIST ATAAQSDLNF
INDEGDTFPL RTYGMFSVDF TDEAASESLN VGKVKVHLDS TQVKMPEHVP MMKLWSLNPD
TGLWEEEGDF RFESQRRKRR EDRTFLVGNM EIRERRLFNL DVPESRRCFI KVRAYRSERF
LPSEQIQGVV VSVINLEPRA GFSSNPRAWG RFDSVLTGPN GACLPAFCDD QSPDAYSAYV
LASLAGEELE AVESSPKFNP NAIGVPQPYL NKLKYRRTDH EDPRVKKTAF QISMAKPRPN
SAEESNGPIY AFENLQACEE APPSAAHFRF YQIEGDRYDY NTVPFNEDDP MSWTEDYLAW
WPKPMEFRAC YIKVKIVGPL EVNVRSRNMG GTHRQTVGKL YGIRDVKSTR DRDQPNVSSA
CLEFKCSGML YDQDRVDRTL VKVIPQGSCH RASVNSMLHE YLVNHLPLAV NNDTSEYTML
APLDPLGHNY GIYTVTDQDP RTAKEIALGR CFDGSSDGSS RVMKSNVGVA LTFNCVERQV
GRQSAFQYLQ STSARPSPAS TVRGRAPSRR QRASSGSQRQ PRGVASLRFP GVAQQPLSN
