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P49747

- COMP_HUMAN

UniProt

P49747 - COMP_HUMAN

Protein

Cartilage oligomeric matrix protein

Gene

COMP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 By similarity.By similarity

    Cofactori

    Binds 11-14 calcium ions per subunit.

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. collagen binding Source: UniProtKB
    3. extracellular matrix structural constituent Source: ProtInc
    4. heparan sulfate proteoglycan binding Source: UniProtKB
    5. heparin binding Source: UniProtKB
    6. protease binding Source: BHF-UCL
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. extracellular matrix organization Source: Reactome
    4. growth plate cartilage development Source: Ensembl
    5. limb development Source: UniProtKB
    6. negative regulation of apoptotic process Source: UniProtKB
    7. organ morphogenesis Source: ProtInc
    8. skeletal system development Source: ProtInc

    Keywords - Biological processi

    Apoptosis, Cell adhesion

    Keywords - Ligandi

    Calcium, Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cartilage oligomeric matrix protein
    Short name:
    COMP
    Alternative name(s):
    Thrombospondin-5
    Short name:
    TSP5
    Gene namesi
    Name:COMP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2227. COMP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671G → E in EDM1. 1 Publication
    VAR_066789
    Natural varianti276 – 2761P → R in EDM1. 2 Publications
    VAR_026239
    Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
    VAR_066792
    Natural varianti311 – 3111A → D in EDM1. 1 Publication
    VAR_066793
    Natural varianti317 – 3171D → G in EDM1; atypical form. 1 Publication
    VAR_066794
    Natural varianti326 – 3261D → G in EDM1. 1 Publication
    VAR_066795
    Natural varianti342 – 3421D → Y in EDM1; Fairbank type. 2 Publications
    VAR_007617
    Natural varianti348 – 3481C → F in EDM1. 1 Publication
    VAR_066798
    Natural varianti361 – 3611D → V in EDM1; Fairbank type.
    VAR_007619
    Natural varianti361 – 3611D → Y in EDM1; binds less calcium. 1 Publication
    VAR_007620
    Natural varianti367 – 3682Missing in EDM1.
    VAR_007621
    Natural varianti371 – 3711C → S in EDM1; Fairbank type. 2 Publications
    VAR_007622
    Natural varianti371 – 3711C → Y in EDM1. 1 Publication
    VAR_066800
    Natural varianti374 – 3741D → N in EDM1. 1 Publication
    VAR_066801
    Natural varianti376 – 3761D → N in EDM1. 1 Publication
    VAR_066802
    Natural varianti385 – 3851D → N in EDM1; atypical form. 1 Publication
    VAR_066804
    Natural varianti385 – 3851D → Y in EDM1; atypical form. 1 Publication
    VAR_066805
    Natural varianti385 – 3851Missing in EDM1. 1 Publication
    VAR_066806
    Natural varianti397 – 3971D → H in EDM1. 1 Publication
    VAR_066808
    Natural varianti404 – 4041G → R in EDM1. 1 Publication
    VAR_066810
    Natural varianti408 – 4081D → Y in EDM1. 1 Publication
    VAR_007627
    Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
    VAR_066811
    Natural varianti415 – 4151N → K in EDM1. 1 Publication
    VAR_066812
    Natural varianti420 – 4201D → A in EDM1. 1 Publication
    VAR_026240
    Natural varianti427 – 4271G → E in EDM1. 1 Publication
    VAR_066813
    Natural varianti430 – 4323CDS → LWC in EDM1.
    VAR_066814
    Natural varianti453 – 4531N → S in EDM1; Fairbank type. 1 Publication
    Corresponds to variant rs28936668 [ dbSNP | Ensembl ].
    VAR_007630
    Natural varianti457 – 4571Missing in EDM1. 1 Publication
    VAR_066817
    Natural varianti473 – 4731D → DD in EDM1. 1 Publication
    VAR_066818
    Natural varianti501 – 5011G → D in EDM1. 1 Publication
    VAR_066821
    Natural varianti523 – 5231N → K in EDM1; Ribbing type. 2 Publications
    VAR_007640
    Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
    VAR_007641
    Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
    VAR_007642
    Natural varianti718 – 7181R → P in EDM1. 1 Publication
    VAR_066826
    Natural varianti718 – 7181R → W in EDM1. 1 Publication
    Corresponds to variant rs28936368 [ dbSNP | Ensembl ].
    VAR_066827
    Pseudoachondroplasia (PSACH) [MIM:177170]: A skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341P → S in PSACH. 1 Publication
    VAR_066790
    Natural varianti290 – 2901D → G in PSACH. 1 Publication
    VAR_066791
    Natural varianti290 – 2901D → N in PSACH; mild form.
    VAR_007614
    Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
    VAR_066792
    Natural varianti299 – 2991G → R in PSACH. 1 Publication
    VAR_007615
    Natural varianti326 – 3261D → Y in PSACH. 1 Publication
    VAR_066796
    Natural varianti328 – 3281C → R in PSACH; mild form. 2 Publications
    VAR_007616
    Natural varianti341 – 3422Missing in PSACH.
    VAR_066797
    Natural varianti348 – 3481C → R in PSACH. 1 Publication
    VAR_017102
    Natural varianti349 – 3491D → V in PSACH; mild form.
    VAR_007618
    Natural varianti350 – 37223Missing in PSACH.
    VAR_066799Add
    BLAST
    Natural varianti372 – 3721Missing in PSACH. 1 Publication
    VAR_007623
    Natural varianti374 – 3741Missing in PSACH; mild form.
    VAR_007624
    Natural varianti378 – 3781D → V in PSACH. 1 Publication
    VAR_066803
    Natural varianti387 – 3871C → G in PSACH; mild form.
    VAR_007625
    Natural varianti387 – 3871C → R in PSACH. 1 Publication
    VAR_066807
    Natural varianti391 – 3944PNSD → V in PSACH.
    VAR_007626
    Natural varianti402 – 4043GIG → VC in PSACH.
    VAR_066809
    Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
    VAR_066811
    Natural varianti440 – 4401G → E in PSACH; mild form.
    VAR_007628
    Natural varianti440 – 4401G → R in PSACH. 2 Publications
    VAR_007629
    Natural varianti446 – 4461D → N in PSACH. 1 Publication
    VAR_066815
    Natural varianti448 – 4481C → S in PSACH. 1 Publication
    VAR_066816
    Natural varianti459 – 4591Missing in PSACH; severe form. 2 Publications
    VAR_007631
    Natural varianti468 – 4681C → Y in PSACH; severe form. 2 Publications
    VAR_007632
    Natural varianti469 – 4691Missing in PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen. 1 Publication
    VAR_007633
    Natural varianti472 – 4721D → Y in PSACH; severe form. 2 Publications
    VAR_007634
    Natural varianti473 – 4731D → G in PSACH; severe form.
    Corresponds to variant rs28936669 [ dbSNP | Ensembl ].
    VAR_007635
    Natural varianti473 – 4731D → H in PSACH. 1 Publication
    VAR_066819
    Natural varianti473 – 4731Missing in PSACH; severe form. 1 Publication
    VAR_007636
    Natural varianti475 – 4751D → N in PSACH. 1 Publication
    VAR_066820
    Natural varianti482 – 4821D → G in PSACH. 2 Publications
    VAR_007637
    Natural varianti507 – 5071D → G in PSACH. 1 Publication
    VAR_066822
    Natural varianti511 – 5111D → G in PSACH. 1 Publication
    VAR_066823
    Natural varianti513 – 5164Missing in PSACH; mild form. 1 Publication
    VAR_007638
    Natural varianti515 – 5151D → G in PSACH. 1 Publication
    VAR_066824
    Natural varianti518 – 5181D → N in PSACH; mild form.
    VAR_007639
    Natural varianti529 – 5291T → I in PSACH. 1 Publication
    VAR_066825
    Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
    VAR_007641
    Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
    VAR_007642
    Natural varianti719 – 7191G → D in PSACH; severe. 1 Publication
    VAR_017103
    Natural varianti719 – 7191G → S in PSACH. 1 Publication
    VAR_066828

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi132400. phenotype.
    177170. phenotype.
    Orphaneti93308. Multiple epiphyseal dysplasia type 1.
    750. Pseudoachondroplasia.
    PharmGKBiPA26744.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 757737Cartilage oligomeric matrix proteinPRO_0000035857Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi69 – 69Interchain1 Publication
    Disulfide bondi72 – 72Interchain1 Publication
    Disulfide bondi91 ↔ 102PROSITE-ProRule annotation
    Disulfide bondi96 ↔ 111PROSITE-ProRule annotation
    Disulfide bondi114 ↔ 125PROSITE-ProRule annotation
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi131 ↔ 142PROSITE-ProRule annotation
    Disulfide bondi136 ↔ 151PROSITE-ProRule annotation
    Disulfide bondi154 ↔ 178PROSITE-ProRule annotation
    Disulfide bondi184 ↔ 197PROSITE-ProRule annotation
    Disulfide bondi191 ↔ 206PROSITE-ProRule annotation
    Disulfide bondi209 ↔ 221PROSITE-ProRule annotation
    Disulfide bondi229 ↔ 2431 PublicationPROSITE-ProRule annotation
    Disulfide bondi237 ↔ 2531 PublicationPROSITE-ProRule annotation
    Disulfide bondi255 ↔ 2661 PublicationPROSITE-ProRule annotation
    Disulfide bondi282 ↔ 2871 PublicationPROSITE-ProRule annotation
    Disulfide bondi292 ↔ 3121 PublicationPROSITE-ProRule annotation
    Disulfide bondi328 ↔ 3481 PublicationPROSITE-ProRule annotation
    Disulfide bondi351 ↔ 3711 PublicationPROSITE-ProRule annotation
    Disulfide bondi387 ↔ 4071 PublicationPROSITE-ProRule annotation
    Disulfide bondi410 ↔ 4301 PublicationPROSITE-ProRule annotation
    Disulfide bondi448 ↔ 4681 PublicationPROSITE-ProRule annotation
    Disulfide bondi484 ↔ 5041 PublicationPROSITE-ProRule annotation
    Disulfide bondi520 ↔ 7411 PublicationPROSITE-ProRule annotation
    Glycosylationi742 – 7421N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP49747.
    PaxDbiP49747.
    PRIDEiP49747.

    PTM databases

    PhosphoSiteiP49747.

    Miscellaneous databases

    PMAP-CutDBP49747.

    Expressioni

    Tissue specificityi

    Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect.1 Publication

    Developmental stagei

    Present during the earliest stages of limb maturation and is later found in regions where the joints develop.1 Publication

    Gene expression databases

    ArrayExpressiP49747.
    BgeeiP49747.
    CleanExiHS_COMP.
    GenevestigatoriP49747.

    Interactioni

    Subunit structurei

    Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca2+, Mg2+ or Mn2+). The greatest amount of binding is seen in the presence of Mn2+. Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACANP136082EBI-2531022,EBI-6259246From a different organism.
    ADAMTS12P583973EBI-2531022,EBI-9028051

    Protein-protein interaction databases

    IntActiP49747. 4 interactions.
    STRINGi9606.ENSP00000222271.

    Structurei

    Secondary structure

    1
    757
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi232 – 2343
    Beta strandi241 – 2455
    Beta strandi251 – 2555
    Beta strandi259 – 2657
    Beta strandi272 – 2743
    Helixi285 – 2873
    Beta strandi291 – 2955
    Beta strandi306 – 3083
    Helixi310 – 3123
    Turni314 – 3174
    Beta strandi319 – 3213
    Helixi323 – 3253
    Beta strandi327 – 3315
    Beta strandi342 – 3443
    Helixi346 – 3483
    Beta strandi364 – 3674
    Helixi369 – 3713
    Beta strandi378 – 3803
    Beta strandi401 – 4033
    Helixi405 – 4073
    Beta strandi424 – 4263
    Turni428 – 4303
    Helixi443 – 4453
    Beta strandi462 – 4643
    Turni466 – 4683
    Beta strandi470 – 4734
    Beta strandi475 – 4773
    Helixi479 – 4813
    Beta strandi495 – 5006
    Turni503 – 5064
    Beta strandi511 – 5133
    Helixi515 – 5173
    Beta strandi532 – 5409
    Beta strandi551 – 5533
    Turni555 – 5573
    Beta strandi560 – 5623
    Beta strandi567 – 58822
    Beta strandi596 – 60510
    Beta strandi608 – 61710
    Beta strandi625 – 6273
    Beta strandi636 – 6416
    Helixi648 – 6558
    Beta strandi656 – 6583
    Turni661 – 6633
    Beta strandi664 – 6696
    Beta strandi681 – 6899
    Helixi690 – 6923
    Beta strandi694 – 7018
    Beta strandi704 – 7085
    Beta strandi716 – 72813
    Beta strandi732 – 74110
    Helixi748 – 7547

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FBYX-ray3.15A/B/C225-757[»]
    ProteinModelPortaliP49747.
    SMRiP49747. Positions 29-72, 91-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49747.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 12640EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini127 – 17953EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini180 – 22243EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini225 – 26743EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Repeati268 – 30033TSP type-3 1Add
    BLAST
    Repeati301 – 33636TSP type-3 2Add
    BLAST
    Repeati337 – 35923TSP type-3 3Add
    BLAST
    Repeati360 – 39536TSP type-3 4Add
    BLAST
    Repeati396 – 41823TSP type-3 5Add
    BLAST
    Repeati419 – 45638TSP type-3 6Add
    BLAST
    Repeati457 – 49236TSP type-3 7Add
    BLAST
    Repeati493 – 52836TSP type-3 8Add
    BLAST
    Domaini532 – 746215TSP C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 8665COMP N-terminalAdd
    BLAST
    Regioni527 – 757231Mediates cell survival and induction of the IAP family of survival proteinsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi367 – 3693Cell attachment siteSequence Analysis

    Domaini

    The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response.1 Publication
    The TSP C-terminal domain mediates interaction with FN1 and ACAN.1 Publication
    Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions.1 Publication

    Sequence similaritiesi

    Belongs to the thrombospondin family.Curated
    Contains 4 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
    Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000007542.
    HOVERGENiHBG000636.
    InParanoidiP49747.
    KOiK04659.
    OMAiPEDYETQ.
    PhylomeDBiP49747.
    TreeFamiTF324917.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    4.10.1080.10. 2 hits.
    InterProiIPR028492. Comp.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR024665. Thbs/COMP_coiled-coil.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR017897. Thrombospondin_3_rpt.
    IPR008859. Thrombospondin_C.
    IPR028974. TSP_type-3_rpt.
    [Graphical view]
    PANTHERiPTHR10199:SF81. PTHR10199:SF81. 1 hit.
    PfamiPF11598. COMP. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF02412. TSP_3. 6 hits.
    PF05735. TSP_C. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 2 hits.
    SM00179. EGF_CA. 2 hits.
    [Graphical view]
    SUPFAMiSSF103647. SSF103647. 3 hits.
    SSF49899. SSF49899. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 3 hits.
    PS01187. EGF_CA. 2 hits.
    PS51234. TSP3. 8 hits.
    PS51236. TSP_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49747-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE    50
    LLRQQVREIT FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV 100
    ACIQTESGAR CGPCPAGFTG NGSHCTDVNE CNAHPCFPRV RCINTSPGFR 150
    CEACPPGYSG PTHQGVGLAF AKANKQVCTD INECETGQHN CVPNSVCINT 200
    RGSFQCGPCQ PGFVGDQASG CQRRAQRFCP DGSPSECHEH ADCVLERDGS 250
    RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ 300
    EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN 350
    CRSQKNDDQK DTDQDGRGDA CDDDIDGDRI RNQADNCPRV PNSDQKDSDG 400
    DGIGDACDNC PQKSNPDQAD VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT 450
    VPNSAQEDSD HDGQGDACDD DDDNDGVPDS RDNCRLVPNP GQEDADRDGV 500
    GDVCQDDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD PEGDAQIDPN 550
    WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI 600
    FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL 650
    RNALWHTGDT ESQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY 700
    EGPELVADSN VVLDTTMRGG RLGVFCFSQE NIIWANLRYR CNDTIPEDYE 750
    THQLRQA 757
    Length:757
    Mass (Da):82,860
    Last modified:October 14, 2008 - v2
    Checksum:iA0B73AADB39FBC7B
    GO
    Isoform 2 (identifier: P49747-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         129-181: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:704
    Mass (Da):77,214
    Checksum:i1126EE4088275D29
    GO

    Sequence cautioni

    The sequence AAB86501.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561A → R in AAA57253. (PubMed:7713493)Curated
    Sequence conflicti256 – 2561A → R in BAC53888. 1 PublicationCurated
    Sequence conflicti340 – 3401D → Y in AAB35270. (PubMed:7670472)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501E → D.2 Publications
    VAR_016254
    Natural varianti51 – 511L → W.2 Publications
    VAR_016255
    Natural varianti109 – 1091A → G.2 Publications
    VAR_016257
    Natural varianti167 – 1671G → E in EDM1. 1 Publication
    VAR_066789
    Natural varianti224 – 2241R → G.2 Publications
    VAR_016258
    Natural varianti234 – 2341P → S in PSACH. 1 Publication
    VAR_066790
    Natural varianti276 – 2761P → R in EDM1. 2 Publications
    VAR_026239
    Natural varianti285 – 2851R → P.2 Publications
    VAR_016261
    Natural varianti290 – 2901D → G in PSACH. 1 Publication
    VAR_066791
    Natural varianti290 – 2901D → N in PSACH; mild form.
    VAR_007614
    Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
    VAR_066792
    Natural varianti299 – 2991G → R in PSACH. 1 Publication
    VAR_007615
    Natural varianti311 – 3111A → D in EDM1. 1 Publication
    VAR_066793
    Natural varianti317 – 3171D → G in EDM1; atypical form. 1 Publication
    VAR_066794
    Natural varianti326 – 3261D → G in EDM1. 1 Publication
    VAR_066795
    Natural varianti326 – 3261D → Y in PSACH. 1 Publication
    VAR_066796
    Natural varianti328 – 3281C → R in PSACH; mild form. 2 Publications
    VAR_007616
    Natural varianti341 – 3422Missing in PSACH.
    VAR_066797
    Natural varianti342 – 3421D → Y in EDM1; Fairbank type. 2 Publications
    VAR_007617
    Natural varianti348 – 3481C → F in EDM1. 1 Publication
    VAR_066798
    Natural varianti348 – 3481C → R in PSACH. 1 Publication
    VAR_017102
    Natural varianti349 – 3491D → V in PSACH; mild form.
    VAR_007618
    Natural varianti350 – 37223Missing in PSACH.
    VAR_066799Add
    BLAST
    Natural varianti361 – 3611D → V in EDM1; Fairbank type.
    VAR_007619
    Natural varianti361 – 3611D → Y in EDM1; binds less calcium. 1 Publication
    VAR_007620
    Natural varianti367 – 3682Missing in EDM1.
    VAR_007621
    Natural varianti371 – 3711C → S in EDM1; Fairbank type. 2 Publications
    VAR_007622
    Natural varianti371 – 3711C → Y in EDM1. 1 Publication
    VAR_066800
    Natural varianti372 – 3721Missing in PSACH. 1 Publication
    VAR_007623
    Natural varianti374 – 3741D → N in EDM1. 1 Publication
    VAR_066801
    Natural varianti374 – 3741Missing in PSACH; mild form.
    VAR_007624
    Natural varianti376 – 3761D → N in EDM1. 1 Publication
    VAR_066802
    Natural varianti378 – 3781D → V in PSACH. 1 Publication
    VAR_066803
    Natural varianti381 – 3811R → C.
    Corresponds to variant rs3179763 [ dbSNP | Ensembl ].
    VAR_046796
    Natural varianti385 – 3851D → N in EDM1; atypical form. 1 Publication
    VAR_066804
    Natural varianti385 – 3851D → Y in EDM1; atypical form. 1 Publication
    VAR_066805
    Natural varianti385 – 3851Missing in EDM1. 1 Publication
    VAR_066806
    Natural varianti387 – 3871C → G in PSACH; mild form.
    VAR_007625
    Natural varianti387 – 3871C → R in PSACH. 1 Publication
    VAR_066807
    Natural varianti391 – 3944PNSD → V in PSACH.
    VAR_007626
    Natural varianti397 – 3971D → H in EDM1. 1 Publication
    VAR_066808
    Natural varianti402 – 4043GIG → VC in PSACH.
    VAR_066809
    Natural varianti404 – 4041G → R in EDM1. 1 Publication
    VAR_066810
    Natural varianti408 – 4081D → Y in EDM1. 1 Publication
    VAR_007627
    Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
    VAR_066811
    Natural varianti415 – 4151N → K in EDM1. 1 Publication
    VAR_066812
    Natural varianti420 – 4201D → A in EDM1. 1 Publication
    VAR_026240
    Natural varianti427 – 4271G → E in EDM1. 1 Publication
    VAR_066813
    Natural varianti430 – 4323CDS → LWC in EDM1.
    VAR_066814
    Natural varianti440 – 4401G → E in PSACH; mild form.
    VAR_007628
    Natural varianti440 – 4401G → R in PSACH. 2 Publications
    VAR_007629
    Natural varianti446 – 4461D → N in PSACH. 1 Publication
    VAR_066815
    Natural varianti448 – 4481C → S in PSACH. 1 Publication
    VAR_066816
    Natural varianti453 – 4531N → S in EDM1; Fairbank type. 1 Publication
    Corresponds to variant rs28936668 [ dbSNP | Ensembl ].
    VAR_007630
    Natural varianti457 – 4571Missing in EDM1. 1 Publication
    VAR_066817
    Natural varianti459 – 4591Missing in PSACH; severe form. 2 Publications
    VAR_007631
    Natural varianti468 – 4681C → Y in PSACH; severe form. 2 Publications
    VAR_007632
    Natural varianti469 – 4691Missing in PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen. 1 Publication
    VAR_007633
    Natural varianti472 – 4721D → Y in PSACH; severe form. 2 Publications
    VAR_007634
    Natural varianti473 – 4731D → DD in EDM1. 1 Publication
    VAR_066818
    Natural varianti473 – 4731D → G in PSACH; severe form.
    Corresponds to variant rs28936669 [ dbSNP | Ensembl ].
    VAR_007635
    Natural varianti473 – 4731D → H in PSACH. 1 Publication
    VAR_066819
    Natural varianti473 – 4731Missing in PSACH; severe form. 1 Publication
    VAR_007636
    Natural varianti475 – 4751D → N in PSACH. 1 Publication
    VAR_066820
    Natural varianti482 – 4821D → G in PSACH. 2 Publications
    VAR_007637
    Natural varianti501 – 5011G → D in EDM1. 1 Publication
    VAR_066821
    Natural varianti507 – 5071D → G in PSACH. 1 Publication
    VAR_066822
    Natural varianti511 – 5111D → G in PSACH. 1 Publication
    VAR_066823
    Natural varianti513 – 5164Missing in PSACH; mild form. 1 Publication
    VAR_007638
    Natural varianti515 – 5151D → G in PSACH. 1 Publication
    VAR_066824
    Natural varianti518 – 5181D → N in PSACH; mild form.
    VAR_007639
    Natural varianti523 – 5231N → K in EDM1; Ribbing type. 2 Publications
    VAR_007640
    Natural varianti529 – 5291T → I in PSACH. 1 Publication
    VAR_066825
    Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
    VAR_007641
    Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
    VAR_007642
    Natural varianti718 – 7181R → P in EDM1. 1 Publication
    VAR_066826
    Natural varianti718 – 7181R → W in EDM1. 1 Publication
    Corresponds to variant rs28936368 [ dbSNP | Ensembl ].
    VAR_066827
    Natural varianti719 – 7191G → D in PSACH; severe. 1 Publication
    VAR_017103
    Natural varianti719 – 7191G → S in PSACH. 1 Publication
    VAR_066828
    Natural varianti756 – 7561Q → R in a patient with multiple epiphyseal dysplasia. 1 Publication
    Corresponds to variant rs61752496 [ dbSNP | Ensembl ].
    VAR_066829

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei129 – 18153Missing in isoform 2. 1 PublicationVSP_055758Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32137 mRNA. Translation: AAA57253.1.
    AB086984 mRNA. Translation: BAC53888.1.
    AK296586 mRNA. Translation: BAG59205.1.
    AC003107 Genomic DNA. Translation: AAB86501.1. Sequence problems.
    CH471106 Genomic DNA. Translation: EAW84737.1.
    BC110847 mRNA. Translation: AAI10848.1.
    BC125092 mRNA. Translation: AAI25093.1.
    S79499 Genomic DNA. Translation: AAB35269.1.
    S79500 Genomic DNA. Translation: AAB35270.1.
    CCDSiCCDS12385.1.
    RefSeqiNP_000086.2. NM_000095.2.
    UniGeneiHs.1584.

    Genome annotation databases

    EnsembliENST00000222271; ENSP00000222271; ENSG00000105664. [P49747-1]
    ENST00000425807; ENSP00000403792; ENSG00000105664. [P49747-2]
    GeneIDi1311.
    KEGGihsa:1311.
    UCSCiuc002nkd.3. human.

    Polymorphism databases

    DMDMi209572601.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32137 mRNA. Translation: AAA57253.1 .
    AB086984 mRNA. Translation: BAC53888.1 .
    AK296586 mRNA. Translation: BAG59205.1 .
    AC003107 Genomic DNA. Translation: AAB86501.1 . Sequence problems.
    CH471106 Genomic DNA. Translation: EAW84737.1 .
    BC110847 mRNA. Translation: AAI10848.1 .
    BC125092 mRNA. Translation: AAI25093.1 .
    S79499 Genomic DNA. Translation: AAB35269.1 .
    S79500 Genomic DNA. Translation: AAB35270.1 .
    CCDSi CCDS12385.1.
    RefSeqi NP_000086.2. NM_000095.2.
    UniGenei Hs.1584.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FBY X-ray 3.15 A/B/C 225-757 [» ]
    ProteinModelPortali P49747.
    SMRi P49747. Positions 29-72, 91-757.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49747. 4 interactions.
    STRINGi 9606.ENSP00000222271.

    PTM databases

    PhosphoSitei P49747.

    Polymorphism databases

    DMDMi 209572601.

    Proteomic databases

    MaxQBi P49747.
    PaxDbi P49747.
    PRIDEi P49747.

    Protocols and materials databases

    DNASUi 1311.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222271 ; ENSP00000222271 ; ENSG00000105664 . [P49747-1 ]
    ENST00000425807 ; ENSP00000403792 ; ENSG00000105664 . [P49747-2 ]
    GeneIDi 1311.
    KEGGi hsa:1311.
    UCSCi uc002nkd.3. human.

    Organism-specific databases

    CTDi 1311.
    GeneCardsi GC19M018894.
    GeneReviewsi COMP.
    H-InvDB HIX0014925.
    HGNCi HGNC:2227. COMP.
    MIMi 132400. phenotype.
    177170. phenotype.
    600310. gene.
    neXtProti NX_P49747.
    Orphaneti 93308. Multiple epiphyseal dysplasia type 1.
    750. Pseudoachondroplasia.
    PharmGKBi PA26744.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000007542.
    HOVERGENi HBG000636.
    InParanoidi P49747.
    KOi K04659.
    OMAi PEDYETQ.
    PhylomeDBi P49747.
    TreeFami TF324917.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    ChiTaRSi COMP. human.
    EvolutionaryTracei P49747.
    GeneWikii Cartilage_oligomeric_matrix_protein.
    GenomeRNAii 1311.
    NextBioi 5361.
    PMAP-CutDB P49747.
    PROi P49747.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49747.
    Bgeei P49747.
    CleanExi HS_COMP.
    Genevestigatori P49747.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    4.10.1080.10. 2 hits.
    InterProi IPR028492. Comp.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR024665. Thbs/COMP_coiled-coil.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR017897. Thrombospondin_3_rpt.
    IPR008859. Thrombospondin_C.
    IPR028974. TSP_type-3_rpt.
    [Graphical view ]
    PANTHERi PTHR10199:SF81. PTHR10199:SF81. 1 hit.
    Pfami PF11598. COMP. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF02412. TSP_3. 6 hits.
    PF05735. TSP_C. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 2 hits.
    SM00179. EGF_CA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF103647. SSF103647. 3 hits.
    SSF49899. SSF49899. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 3 hits.
    PS01187. EGF_CA. 2 hits.
    PS51234. TSP3. 8 hits.
    PS51236. TSP_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of human and mouse cartilage oligomeric matrix protein."
      Newton G., Weremowicz S., Morton C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Lawler J.
      Genomics 24:435-439(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
      Tissue: Cartilage.
    2. "Human comp cDNA with 5 SNIPs."
      Hashimoto Y., Mori H.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M.,