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 27-NOV-2024, entry version 161. 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}. 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; 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; 26. DR STRING; 9606.ENSP00000291495; -. DR GlyCosmos; Q8IUL8; 3 sites, No reported glycans. DR GlyGen; Q8IUL8; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8IUL8; -. DR PhosphoSitePlus; Q8IUL8; -. DR BioMuta; CILP2; -. DR DMDM; 68565198; -. DR jPOST; Q8IUL8; -. DR MassIVE; Q8IUL8; -. DR PaxDb; 9606-ENSP00000291495; -. DR PeptideAtlas; Q8IUL8; -. DR ProteomicsDB; 70584; -. DR Antibodypedia; 48010; 76 antibodies from 18 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 AGR; HGNC:24213; -. DR CTD; 148113; -. DR DisGeNET; 148113; -. DR GeneCards; CILP2; -. DR HGNC; HGNC:24213; CILP2. DR HPA; ENSG00000160161; Tissue enhanced (ovary, 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; CGVRRME; -. DR OrthoDB; 5383253at2759; -. DR PhylomeDB; Q8IUL8; -. DR TreeFam; TF330132; -. DR PathwayCommons; Q8IUL8; -. DR SignaLink; Q8IUL8; -. DR BioGRID-ORCS; 148113; 19 hits in 1146 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 98 other cell types or tissues. DR ExpressionAtlas; Q8IUL8; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR FunFam; 2.20.100.10:FF:000051; Cartilage intermediate layer protein 2; 1. DR FunFam; 2.60.40.10:FF:001254; Cartilage intermediate layer protein 2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 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:SF0; CARTILAGE INTERMEDIATE LAYER PROTEIN 2; 1. DR PANTHER; PTHR15031; CARTILAGE INTERMEDIATE LAYER PROTEIN CLIP; 1. DR Pfam; PF13620; CarboxypepD_reg; 1. DR Pfam; PF13927; Ig_3; 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; SSF49464; Carboxypeptidase regulatory domain-like; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 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; Proteomics identification; KW 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 //