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Q9R1N9 (CODA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XIII) chain
Gene names
Name:Col13a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length751 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. Ref.3 Ref.4 Ref.6 UniProtKB Q5TAT6

Subunit structure

Homotrimer; disulfide-linked. Nucleation of the type XIII collagen triple helix is likely to occur at the N-terminal region with triple helix formation proceeding from the N- to the C-terminus. Interacts with FN1, perlecan/HSPG2 and NID2 By similarity. UniProtKB Q5TAT6

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.1.

Developmental stage

Expression levels remain fairly constant during early fetal development. This is followed by a marked increase of expression levels during the final stages of organogenesis, with initiation of the rapid fetal growth phase before birth. At mid-gestation, strongly expressed in the central and peripheral nervous systems. Also strongly expressed in developing heart, with localization to cell-cell contacts and accentuated in intercalated disks perinatally. During late fetal development, expressed in many tissues including cartilage, bone, skeletal muscle, lung, intestine and skin. Not detected in endothelia of most blood vessels or the endocardium of the heart. Ref.5

Miscellaneous

Transgenic mice overexpressing COL13A1 with a 90 amino acid in-frame deletion of the COL2 sequence show embryonic lethality due either to a lack of placental formation or to cardiovascular defects in offspring from heterozygous mating. In contrast, transgenic mice expressing an N-terminally altered COL13A1 lacking both cytosolic and transmembrane domains while retaining the collagenous ectodomain are viable and fertile, but display progressive muscular myopathy. Ref.3 Ref.4

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms may exist.
Isoform 1 Ref.2 (identifier: Q9R1N9-1)

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.
Isoform 2 Ref.1 (identifier: Q9R1N9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     651-662: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 751751Collagen alpha-1(XIII) chain
PRO_0000284680

Regions

Topological domain1 – 4040Cytoplasmic Potential
Transmembrane41 – 5919Helical; Signal-anchor for type II membrane protein; Potential
Topological domain60 – 751692Extracellular Potential
Region1 – 119119Nonhelical region 1 (NC1)
Region120 – 223104Triple-helical region 1 (COL1)
Region224 – 27350Nonhelical region 2 (NC2)
Region274 – 445172Triple-helical region 2 (COL2)
Region446 – 46722Nonhelical region 3 (NC3)
Region468 – 733266Triple-helical region 3 (COL3)
Region734 – 75118Nonhelical region 4 (NC4)

Amino acid modifications

Glycosylation4511N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence651 – 66212Missing in isoform 2. Ref.1
VSP_052388

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FBE2443E1CBF51AD

FASTA75173,172
        10         20         30         40         50         60 
MVAERTRKAA ASGSRGPGEL GAPGPGTVAL AEQCARLPSP GCCGLLALAL CSLALSLLAH 

        70         80         90        100        110        120 
FRTAELQARV LRLEAERGEQ QMEKAILGRV NQLLDEKWKF YSRRRREAPK MSPGCNCPPG 

       130        140        150        160        170        180 
PPGPTGRPGL PGDKGAIGMP GRVGIKGQPG EKGAPGDAGM SIVGPRGPPG QPGTRGFPGF 

       190        200        210        220        230        240 
PGPIGLDGRP GHPGPKGEMG LVGPRGQPGP QGQKGEKGQC GEYPHREYPG GMLAALRSNP 

       250        260        270        280        290        300 
IMSLKLLPLL NSVRLAPPPV IKRRTFQGEQ SQTGIQGPPG PPGPPGPSGP LGHPGLPGPI 

       310        320        330        340        350        360 
GPPGLPGPPG PKGDPGIQGY HGRKGERGMP GMPGKHGAKG VPGIAVAGMK GEPGTPGTKG 

       370        380        390        400        410        420 
EKGAAGSPGL LGQKGEKGDA GNAIGGGRGE PGPPGLPGPP GPKGEAGVDG QAGPPGQQGD 

       430        440        450        460        470        480 
KGQPGAAGEQ GPSGPKGAKG EPGKGEMVDY NGSINEALQE IRTLALMGPP GLPGQTGPPG 

       490        500        510        520        530        540 
PPGTPGQRGE IGLPGPPGHD GDKGPRGKPG DMGPAGPQGP PGKDGPPGMK GEVGPPGSPG 

       550        560        570        580        590        600 
EKGETGQAGP QGLDGPTGEK GEPGDEGRPG ATGLPGPIGL PGFTGEKGEA GEKGDPGAEV 

       610        620        630        640        650        660 
PGPPGPEGPP GPPGLQGFPG PKGEAGLEGS KGEKGSQGEK GDRGPLGLPG ASGLDGRPGP 

       670        680        690        700        710        720 
PGTPGPIGVP GPAGPKGERG SKGDPGMTGP TGAAGLPGLH GPPGDKGNRG ERGKKGSRGP 

       730        740        750 
KGDKGDQGAP GLDAPCPLGE DGLPVQGCWN K 

« Hide

Isoform 2 [UniParc].

Checksum: F13951061381F017
Show »

FASTA73972,110

References

[1]"Type XIII collagen is identified as a plasma membrane protein."
Hagg P., Rehn M., Huhtala P., Vaisanen T., Tamminen M., Pihlajaniemi T.
J. Biol. Chem. 273:15590-15597(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
Tissue: Intestine.
[2]"Complete exon-intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue."
Kvist A.-P., Latvanlehto A., Sund M., Horelli-Kuitunen N., Rehn M., Palotie A., Beier D., Pihlajaniemi T.
Matrix Biol. 18:261-274(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[3]"Lack of cytosolic and transmembrane domains of type XIII collagen results in progressive myopathy."
Kvist A.-P., Latvanlehto A., Sund M., Eklund L., Vaisanen T., Hagg P., Sormunen R., Komulainen J., Fassler R., Pihlajaniemi T.
Am. J. Pathol. 159:1581-1592(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TRANSGENIC MICE.
[4]"Abnormal adherence junctions in the heart and reduced angiogenesis in transgenic mice overexpressing mutant type XIII collagen."
Sund M., Ylonen R., Tuomisto A., Sormunen R., Tahkola J., Kvist A.-P., Kontusaari S., Autio-Harmainen H., Pihlajaniemi T.
EMBO J. 20:5153-5164(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TRANSGENIC MICE.
[5]"Distinct expression of type XIII collagen in neuronal structures and other tissues during mouse development."
Sund M., Vaisanen T., Kaukinen S., Ilves M., Tu H., Autio-Harmainen H., Rauvala H., Pihlajaniemi T.
Matrix Biol. 20:215-231(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[6]"Type XIII collagen strongly affects bone formation in transgenic mice."
Ylonen R., Kyronlahti T., Sund M., Ilves M., Lehenkari P., Tuukkanen J., Pihlajaniemi T.
J. Bone Miner. Res. 20:1381-1393(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30292 mRNA. Translation: AAC24314.1.
AF063693 expand/collapse EMBL AC list , AF063666, AF063667, AF063668, AF063669, AF063670, AF063671, AF063672, AF063673, AF063674, AF063675, AF063676, AF063677, AF063678, AF063679, AF063680, AF063681, AF063682, AF063683, AF063684, AF063685, AF063686, AF063687, AF063688, AF063689, AF063690, AF063691, AF063692 Genomic DNA. Translation: AAD50327.1.
RefSeqNP_031757.1. NM_007731.2.
UniGeneMm.300931.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000090141.

PTM databases

PhosphoSiteQ9R1N9.

Proteomic databases

PRIDEQ9R1N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105454; ENSMUSP00000101094; ENSMUSG00000058806. [Q9R1N9-2]
GeneID12817.
KEGGmmu:12817.
UCSCuc007fgn.1. mouse. [Q9R1N9-2]

Organism-specific databases

CTD1305.
MGIMGI:1277201. Col13a1.

Phylogenomic databases

eggNOGNOG254293.
GeneTreeENSGT00750000117303.
HOGENOMHOG000085653.
HOVERGENHBG004933.
InParanoidQ9R1N9.
KOK16617.
OMAKDGPPGV.
PhylomeDBQ9R1N9.
TreeFamTF338175.

Gene expression databases

ArrayExpressQ9R1N9.
BgeeQ9R1N9.
CleanExMM_COL13A1.
GenevestigatorQ9R1N9.

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio282282.
PROQ9R1N9.
SOURCESearch...

Entry information

Entry nameCODA1_MOUSE
AccessionPrimary (citable) accession number: Q9R1N9
Secondary accession number(s): O70575
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot