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Protein

Collagen alpha-1(X) chain

Gene

Col10a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi626Calcium 1By similarity1
Metal bindingi627Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi633Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi634Calcium 1By similarity1
Metal bindingi634Calcium 2; shared with neighboring subunitsBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1442490 Collagen degradation
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-8948216 Collagen chain trimerization

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(X) chain
Gene namesi
Name:Col10a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88445 Col10a1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000577119 – 680Collagen alpha-1(X) chainAdd BLAST662

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Keywords - PTMi

Hydroxylation

Proteomic databases

MaxQBiQ05306
PaxDbiQ05306
PRIDEiQ05306

PTM databases

iPTMnetiQ05306
PhosphoSitePlusiQ05306

Expressioni

Gene expression databases

BgeeiENSMUSG00000039462 Expressed in 72 organ(s), highest expression level in intercostal muscle
CleanExiMM_COL10A1
GenevisibleiQ05306 MM

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

ComplexPortaliCPX-2971 Collagen type X trimer
STRINGi10090.ENSMUSP00000101150

Structurei

3D structure databases

ProteinModelPortaliQ05306
SMRiQ05306
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini547 – 680C1qPROSITE-ProRule annotationAdd BLAST134

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 56Nonhelical region (NC2)Add BLAST38
Regioni57 – 519Triple-helical regionAdd BLAST463
Regioni520 – 680Nonhelical region (NC1)Add BLAST161

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGA1 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00760000118830
HOGENOMiHOG000085653
HOVERGENiHBG108220
InParanoidiQ05306
KOiK19479
OMAiYTKGYLD
OrthoDBiEOG091G0L3Y
PhylomeDBiQ05306
TreeFamiTF334029

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR001073 C1q_dom
IPR008160 Collagen
IPR008983 Tumour_necrosis_fac-like_dom
PfamiView protein in Pfam
PF00386 C1q, 1 hit
PF01391 Collagen, 5 hits
PRINTSiPR00007 COMPLEMNTC1Q
SMARTiView protein in SMART
SM00110 C1Q, 1 hit
SUPFAMiSSF49842 SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS50871 C1Q, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q05306-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLPQIPFLLL MFLTLVHGMF YAERYQTPTG IKGPLASPKT QYFIPYAIKS
60 70 80 90 100
KGIPVRGEQG IPGPPGPTGP RGHPGPSGPP GKPGYGSPGL QGEPGLPGPP
110 120 130 140 150
GISATGKPGL PGPPGKPGER GPYGHKGDIG PAGLPGPRGP PGPPGIPGPA
160 170 180 190 200
GISVPGKPGQ QGLTGAPGPR GFPGEKGAQG APGVNGRKGE TGYGSPGRPG
210 220 230 240 250
ERGLPGPQGP IGPPGPSGVG RRGENGFPGQ PGIKGDRGFP GEMGPSGPPG
260 270 280 290 300
PQGPPGKQGR EGIGKPGAIG SPGQPGIPGE KGHPGAPGIA GPPGAPGFGK
310 320 330 340 350
QGLPGLRGQR GPAGLPGAPG AKGERGPAGH PGEPGLPGSP GNMGPQGPKG
360 370 380 390 400
IPGNHGIPGA KGEIGLVGPA GPPGARGARG PPGLDGKTGY PGEPGLNGPK
410 420 430 440 450
GNPGLPGQKG DPGVGGTPGL RGPVGPVGAK GVPGHNGEAG PRGEPGIPGT
460 470 480 490 500
RGPTGPPGVP GFPGSKGDPG NPGAPGPAGI ATKGLNGPTG PPGPPGPRGH
510 520 530 540 550
SGEPGLPGPP GPPGPPGQAV MPDGFIKAGQ RPRLSGMPLV SANHGVTGMP
560 570 580 590 600
VSAFTVILSK AYPAVGAPIP FDEILYNRQQ HYDPRSGIFT CKIPGIYYFS
610 620 630 640 650
YHVHVKGTHV WVGLYKNGTP TMYTYDEYSK GYLDQASGSA IMELTENDQV
660 670 680
WLQLPNAESN GLYSSEYVHS SFSGFLVAPM
Length:680
Mass (Da):66,775
Last modified:November 1, 1995 - v1
Checksum:iFE984CA99AF708E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13L → F no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti27T → S no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti248P → L no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti248P → L in CAA46237 (PubMed:1587271).Curated1
Sequence conflicti286A → S in CAA79736 (PubMed:8477738).Curated1
Sequence conflicti306L → F no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti306L → F in CAA46237 (PubMed:1587271).Curated1
Sequence conflicti417T → S no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti417T → S in CAA46237 (PubMed:1587271).Curated1
Sequence conflicti451R → K in CAA44741 (PubMed:1543751).Curated1
Sequence conflicti500H → L no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti500H → L in CAA46237 (PubMed:1587271).Curated1
Sequence conflicti567 – 572APIPFD → CPHPIY no nucleotide entry (PubMed:8492743).Curated6
Sequence conflicti567 – 572APIPFD → CPHPIY in CAA46237 (PubMed:1587271).Curated6
Sequence conflicti635Q → T no nucleotide entry (PubMed:8492743).Curated1
Sequence conflicti635Q → T in CAA46237 (PubMed:1587271).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67348 Genomic DNA Translation: CAA47763.1
Z21610 Genomic DNA Translation: CAA79736.1
X65121 Genomic DNA Translation: CAA46237.1
X63013 mRNA Translation: CAA44741.1
CCDSiCCDS23780.1
PIRiS31216
RefSeqiNP_034055.1, NM_009925.4
UniGeneiMm.443177

Genome annotation databases

EnsembliENSMUST00000105511; ENSMUSP00000101150; ENSMUSG00000039462
GeneIDi12813
KEGGimmu:12813
UCSCiuc011xcr.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67348 Genomic DNA Translation: CAA47763.1
Z21610 Genomic DNA Translation: CAA79736.1
X65121 Genomic DNA Translation: CAA46237.1
X63013 mRNA Translation: CAA44741.1
CCDSiCCDS23780.1
PIRiS31216
RefSeqiNP_034055.1, NM_009925.4
UniGeneiMm.443177

3D structure databases

ProteinModelPortaliQ05306
SMRiQ05306
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2971 Collagen type X trimer
STRINGi10090.ENSMUSP00000101150

PTM databases

iPTMnetiQ05306
PhosphoSitePlusiQ05306

Proteomic databases

MaxQBiQ05306
PaxDbiQ05306
PRIDEiQ05306

Protocols and materials databases

DNASUi12813
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000105511; ENSMUSP00000101150; ENSMUSG00000039462
GeneIDi12813
KEGGimmu:12813
UCSCiuc011xcr.1 mouse

Organism-specific databases

CTDi1300
MGIiMGI:88445 Col10a1

Phylogenomic databases

eggNOGiENOG410IGA1 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00760000118830
HOGENOMiHOG000085653
HOVERGENiHBG108220
InParanoidiQ05306
KOiK19479
OMAiYTKGYLD
OrthoDBiEOG091G0L3Y
PhylomeDBiQ05306
TreeFamiTF334029

Enzyme and pathway databases

ReactomeiR-MMU-1442490 Collagen degradation
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

PROiPR:Q05306
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039462 Expressed in 72 organ(s), highest expression level in intercostal muscle
CleanExiMM_COL10A1
GenevisibleiQ05306 MM

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR001073 C1q_dom
IPR008160 Collagen
IPR008983 Tumour_necrosis_fac-like_dom
PfamiView protein in Pfam
PF00386 C1q, 1 hit
PF01391 Collagen, 5 hits
PRINTSiPR00007 COMPLEMNTC1Q
SMARTiView protein in SMART
SM00110 C1Q, 1 hit
SUPFAMiSSF49842 SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS50871 C1Q, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCOAA1_MOUSE
AccessioniPrimary (citable) accession number: Q05306
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 12, 2018
This is version 146 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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