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Q66K08

- CILP1_MOUSE

UniProt

Q66K08 - CILP1_MOUSE

Protein

Cartilage intermediate layer protein 1

Gene

Cilp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage By similarity.By similarity

    GO - Biological processi

    1. negative regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cartilage intermediate layer protein 1
    Short name:
    CILP-1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Cilp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:2444507. Cilp.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 11841163Cartilage intermediate layer protein 1PRO_0000014674Add
    BLAST
    Chaini22 – ?724703Cartilage intermediate layer protein 1 C1PRO_0000014675Add
    BLAST
    Chaini?725 – 1184460Cartilage intermediate layer protein 1 C2PRO_0000014676Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi161 ↔ 195By similarity
    Disulfide bondi165 ↔ 200By similarity
    Disulfide bondi177 ↔ 185By similarity
    Disulfide bondi330 ↔ 376By similarity
    Glycosylationi346 – 3461N-linked (GlcNAc...)By similarity
    Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1000 – 10001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1056 – 10561N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Cleaved into 2 chains possibly by a furin-like protease upon or preceding secretion.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ66K08.
    PRIDEiQ66K08.

    PTM databases

    PhosphoSiteiQ66K08.

    Expressioni

    Gene expression databases

    ArrayExpressiQ66K08.
    BgeeiQ66K08.
    GenevestigatoriQ66K08.

    Interactioni

    Subunit structurei

    Monomer. Interacts with TGFB1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ66K08.
    SMRiQ66K08. Positions 269-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini150 – 20152TSP type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini309 – 39385Ig-like C2-typeAdd
    BLAST

    Sequence similaritiesi

    Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal

    Phylogenomic databases

    eggNOGiNOG38857.
    GeneTreeiENSGT00390000008152.
    HOGENOMiHOG000111676.
    HOVERGENiHBG081175.
    InParanoidiQ66K08.
    OrthoDBiEOG780RKM.
    PhylomeDBiQ66K08.
    TreeFamiTF330132.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    IPR000884. Thrombospondin_1_rpt.
    IPR025155. WxxW_domain.
    [Graphical view]
    PfamiPF13330. Mucin2_WxxW. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view]
    SMARTiSM00408. IGc2. 1 hit.
    SM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS50092. TSP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q66K08-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAIKTWVFS FLVLEVTTVL GRQTMLAQSV RRVQPVKRTP KTLAKPADSQ     50
    ESPGEWTTWF NIDHPGGQGD YERLDAIRFY YGERVCARPL RLEARTTDWM 100
    PAGSTGQVVH GSPREGFWCL NREQRPGQNC SNYTVRFLCP PGSLRGDAEH 150
    IWSSWSPWSK CSAACGHTGV QTRTRTCLAQ TVSLCSEATE EGQLCMSQAC 200
    TACDLTCPMG QVNADCDACM CQDFMLHGAI SLPGGGPAPG AAVYLLAKAP 250
    KMLTRTDSSG RFRVPGLCPD GKTILKITKT KFAPIMITMP KTSLKSATIN 300
    AEFVRAETPY IVMNPEMKAR RAGQSVSLCC KATGKPSPDK YFWYHNNTLL 350
    DPSLYKHESK LVLRNLQQDQ AGEYFCKAQS DAGAVKSKVT QLTVIAHDET 400
    PCNPTPESYL IRLPHDCFQN ASNSFYYDVG RCPIKTCAGQ QDNGIRCRDA 450
    VENCCGISRT EEREIQCSGY TLPTKVAVEC SCQRCAETRS IVRGRVTATD 500
    NGEPMRFGHV YMGNNRVSMT GYKGTFTLHI PQDTERLVLT FVDRLQKFVN 550
    TTKVLPFNKK GSAVFHEIKM LRQKEPITLE AMETNIIPLG EVIGEDPVAE 600
    LEIPSKSFYR QNGEPFTGKV KASVTFLDPR NISTATAAQS DLNFINDEGD 650
    TFPLRTYGMF SVDFRDEATS ESLNAGKVKV HLDSTQVKMP EHVPAMKLWS 700
    LNPDTGLWEE EGDFKFESQR RNKREERTFL VGNMEIRERR LFNLDVPESR 750
    RCFIKVRTYR SERFLPSEQI QGVVVSVINL EPRTGFSSNP RAWGRFDSVI 800
    TGPNGACLPA FCDDQSPDAY SVYVLASLSG EELEAVESSP KFNPNAIGVP 850
    QPYLNKLKYR RTDHEDPRVK KTAFQISMAK PRPNSAEESN GPIYAFENLR 900
    ACEEAPPSAA HFRFYQIEGD RYDYNTVPFN EDDPMSWTED YLAWWPKPME 950
    FRACYIKVKI VGPLEVNVRS RNMGGTHRQT VGKLYGIRDV KSTRDRDQPN 1000
    VSSACLEFKC SGMLYDQDRV DRTLVKVIPQ GSCHRASVNS MLHEYLVNHL 1050
    PLAVNNDTSE YTMLAPLDPL GHNYGIYTVT DQDPRTAKEI ALGRCFDGTS 1100
    DGSSRIMKSN VGVALTFNCA ERQVGRQSAF QYLQSTPARS PATGTVQGRV 1150
    PAMRQQRASR GGLRRRGSMA PLRFSGVAQQ PLSN 1184
    Length:1,184
    Mass (Da):132,334
    Last modified:October 11, 2004 - v1
    Checksum:iC83B97AC0D0DC9D3
    GO

    Sequence cautioni

    The sequence BAC38252.1 differs from that shown. Reason: Frameshift at position 1170.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti499 – 4991T → A(PubMed:16141072)Curated
    Sequence conflicti499 – 4991T → A1 PublicationCurated
    Sequence conflicti734 – 7341M → L in AAM92572. 1 PublicationCurated
    Sequence conflicti1155 – 11551Q → E in AAM92572. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK081544 mRNA. Translation: BAC38252.1. Frameshift.
    BC080666 mRNA. Translation: AAH80666.1.
    AY116589 Genomic DNA. Translation: AAM92571.1.
    AY116591, AY116590 Genomic DNA. Translation: AAM92572.1.
    RefSeqiNP_775561.1. NM_173385.2.
    UniGeneiMm.138455.

    Genome annotation databases

    EnsembliENSMUST00000048762; ENSMUSP00000036631; ENSMUSG00000042254.
    GeneIDi214425.
    KEGGimmu:214425.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK081544 mRNA. Translation: BAC38252.1 . Frameshift.
    BC080666 mRNA. Translation: AAH80666.1 .
    AY116589 Genomic DNA. Translation: AAM92571.1 .
    AY116591 , AY116590 Genomic DNA. Translation: AAM92572.1 .
    RefSeqi NP_775561.1. NM_173385.2.
    UniGenei Mm.138455.

    3D structure databases

    ProteinModelPortali Q66K08.
    SMRi Q66K08. Positions 269-394.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q66K08.

    Proteomic databases

    PaxDbi Q66K08.
    PRIDEi Q66K08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048762 ; ENSMUSP00000036631 ; ENSMUSG00000042254 .
    GeneIDi 214425.
    KEGGi mmu:214425.

    Organism-specific databases

    CTDi 8483.
    MGIi MGI:2444507. Cilp.

    Phylogenomic databases

    eggNOGi NOG38857.
    GeneTreei ENSGT00390000008152.
    HOGENOMi HOG000111676.
    HOVERGENi HBG081175.
    InParanoidi Q66K08.
    OrthoDBi EOG780RKM.
    PhylomeDBi Q66K08.
    TreeFami TF330132.

    Miscellaneous databases

    NextBioi 374308.
    PROi Q66K08.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q66K08.
    Bgeei Q66K08.
    Genevestigatori Q66K08.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    IPR000884. Thrombospondin_1_rpt.
    IPR025155. WxxW_domain.
    [Graphical view ]
    Pfami PF13330. Mucin2_WxxW. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS50092. TSP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NMRI.
      Tissue: Mammary tumor.
    3. "The mouse Cilp gene."
      Lorenzo P., Heinegaard D.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51 AND 344-1184.
      Strain: 129/SvJ.

    Entry informationi

    Entry nameiCILP1_MOUSE
    AccessioniPrimary (citable) accession number: Q66K08
    Secondary accession number(s): Q7TSS0, Q7TSS1, Q8BV01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3