CILP2_HUMAN
ID CILP2_HUMAN Reviewed; 1156 AA.
AC Q8IUL8; Q6NV88; Q8N4A6; Q8WV21;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cartilage intermediate layer protein 2;
DE Short=CILP-2;
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 2 C1;
DE Contains:
DE RecName: Full=Cartilage intermediate layer protein 2 C2;
DE Flags: Precursor;
GN Name=CILP2;
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.
RC TISSUE=Osteoarthritic cartilage;
RX PubMed=12746903; DOI=10.1002/art.10927;
RA Johnson K., Farley D., Hu S.-I., Terkeltaub R.;
RT "One of two chondrocyte-expressed isoforms of cartilage intermediate-layer
RT protein functions as an insulin-like growth factor 1 antagonist.";
RL Arthritis Rheum. 48:1302-1314(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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:0000269|PubMed:21880736}.
CC -!- TISSUE SPECIFICITY: Expressed in articular chondrocytes but not in knee
CC meniscal cartilage cells (PubMed:12746903). Localizes to the
CC intermediate to deep zone of articular cartilage (PubMed:21880736).
CC {ECO:0000269|PubMed:12746903, ECO:0000269|PubMed:21880736}.
CC -!- PTM: May be cleaved into 2 chains possibly by a furin-like protease
CC upon or preceding secretion. {ECO:0000250}.
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DR EMBL; AF542080; AAN17826.1; -; mRNA.
DR EMBL; BC018939; AAH18939.2; -; mRNA.
DR EMBL; BC034926; AAH34926.2; -; mRNA.
DR CCDS; CCDS12405.1; -.
DR RefSeq; NP_694953.2; NM_153221.2.
DR AlphaFoldDB; Q8IUL8; -.
DR BioGRID; 127119; 47.
DR IntAct; Q8IUL8; 4.
DR STRING; 9606.ENSP00000291495; -.
DR GlyGen; Q8IUL8; 3 sites.
DR iPTMnet; Q8IUL8; -.
DR PhosphoSitePlus; Q8IUL8; -.
DR BioMuta; CILP2; -.
DR DMDM; 68565198; -.
DR EPD; Q8IUL8; -.
DR jPOST; Q8IUL8; -.
DR MassIVE; Q8IUL8; -.
DR PaxDb; Q8IUL8; -.
DR PeptideAtlas; Q8IUL8; -.
DR PRIDE; Q8IUL8; -.
DR ProteomicsDB; 70584; -.
DR Antibodypedia; 48010; 82 antibodies from 19 providers.
DR DNASU; 148113; -.
DR Ensembl; ENST00000291495.5; ENSP00000291495.3; ENSG00000160161.9.
DR GeneID; 148113; -.
DR KEGG; hsa:148113; -.
DR MANE-Select; ENST00000291495.5; ENSP00000291495.3; NM_153221.2; NP_694953.2.
DR UCSC; uc002nmv.4; human.
DR CTD; 148113; -.
DR DisGeNET; 148113; -.
DR GeneCards; CILP2; -.
DR HGNC; HGNC:24213; CILP2.
DR HPA; ENSG00000160161; Tissue enhanced (testis).
DR MIM; 612419; gene.
DR neXtProt; NX_Q8IUL8; -.
DR OpenTargets; ENSG00000160161; -.
DR PharmGKB; PA134970563; -.
DR VEuPathDB; HostDB:ENSG00000160161; -.
DR eggNOG; ENOG502QQ8H; Eukaryota.
DR GeneTree; ENSGT00390000008152; -.
DR InParanoid; Q8IUL8; -.
DR OMA; MAGHTEA; -.
DR OrthoDB; 629181at2759; -.
DR PhylomeDB; Q8IUL8; -.
DR TreeFam; TF330132; -.
DR PathwayCommons; Q8IUL8; -.
DR SignaLink; Q8IUL8; -.
DR BioGRID-ORCS; 148113; 18 hits in 1068 CRISPR screens.
DR GenomeRNAi; 148113; -.
DR Pharos; Q8IUL8; Tbio.
DR PRO; PR:Q8IUL8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IUL8; protein.
DR Bgee; ENSG00000160161; Expressed in cartilage tissue and 97 other tissues.
DR ExpressionAtlas; Q8IUL8; baseline and differential.
DR Genevisible; Q8IUL8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
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; SSF49464; SSF49464; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 2: Evidence at transcript 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..1156
FT /note="Cartilage intermediate layer protein 2"
FT /id="PRO_0000014678"
FT CHAIN 21..?709
FT /note="Cartilage intermediate layer protein 2 C1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014679"
FT CHAIN ?710..1156
FT /note="Cartilage intermediate layer protein 2 C2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014680"
FT DOMAIN 146..197
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 292..376
FT /note="Ig-like C2-type"
FT REGION 1134..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..191
FT /evidence="ECO:0000250"
FT DISULFID 162..196
FT /evidence="ECO:0000250"
FT DISULFID 173..181
FT /evidence="ECO:0000250"
FT DISULFID 313..359
FT /evidence="ECO:0000250"
FT CONFLICT 768
FT /note="A -> G (in Ref. 1; AAN17826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1156 AA; 126291 MW; CE4AAB47841C07F9 CRC64;
MASLLPLLCL CVVAAHLAGA RDATPTEEPM ATALGLERRS VYTGQPSPAL EDWEEASEWT
SWFNVDHPGG DGDFESLAAI RFYYGPARVC PRPLALEART TDWALPSAVG ERVHLNPTRG
FWCLNREQPR GRRCSNYHVR FRCPLEASWG AWGPWGPCSG SCGPGRRLRR RHCPSPAGDA
CPGRPLEAQK CVRPRCPGCS LDTCECPDHI LLGSVVTPSG QPLLGARVSL RDQPGTVATS
DAHGTFRVPG VCADSRANIR AQMDGFSAGE AQAQANGSIS VVTIILDKLE KPYLVKHPES
RVREAGQNVT FCCKASGTPM PKKYSWFHNG TLLDRRAHGY GAHLELRGLR PDQAGIYHCK
AWNEAGAVRS GTARLTVLAP GQPACDPRPR EYLIKLPEDC GQPGSGPAYL DVGLCPDTRC
PSLAGSSPRC GDASSRCCSV RRLERREIHC PGYVLPVKVV AECGCQKCLP PRGLVRGRVV
AADSGEPLRF ARILLGQEPI GFTAYQGDFT IEVPPSTQRL VVTFVDPSGE FMDAVRVLPF
DPRGAGVYHE VKAMRKKAPV ILHTSQSNTI PLGELEDEAP LGELVLPSGA FRRADGKPYS
GPVEARVTFV DPRDLTSAAS APSDLRFVDS DGELAPLRTY GMFSVDLRAP GSAEQLQVGP
VAVRVAASQI HMPGHVEALK LWSLNPETGL WEEESGFRRE GSSGPRVRRE ERVFLVGNVE
IRERRLFNLD VPERRRCFVK VRAYANDKFT PSEQVEGVVV TLVNLEPAPG FSANPRAWGR
FDSAVTGPNG ACLPAFCDAD RPDAYTALVT ATLGGEELEP APSLPRPLPA TVGVTQPYLD
RLGYRRTDHD DPAFKRNGFR INLAKPRPGD PAEANGPVYP WRSLRECQGA PVTASHFRFA
RVEADKYEYN VVPFREGTPA SWTGDLLAWW PNPQEFRACF LKVKIQGPQE YMVRSHNAGG
SHPRTRGQLY GLRDARSVRD PERPGTSAAC VEFKCSGMLF DQRQVDRTLV TIMPQGSCRR
VAVNGLLRDY LTRHPPPVPA EDPAAFSMLA PLDPLGHNYG VYTVTDQSPR LAKEIAIGRC
FDGSSDGFSR EMKADAGTAV TFQCREPPAG RPSLFQRLLE SPATALGDIR REMSEAAQAQ
ARASGPLRTR RGRVRQ
