SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9R1N9

- CODA1_MOUSE

UniProt

Q9R1N9 - CODA1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Collagen alpha-1(XIII) chain
Gene
Col13a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.By similarity3 Publications

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. cell-matrix adhesion Source: UniProtKB
  3. endochondral ossification Source: UniProtKB
  4. morphogenesis of a branching structure Source: UniProtKB
  5. single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Differentiation, Osteogenesis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XIII) chain
Gene namesi
Name:Col13a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1277201. Col13a1.

Subcellular locationi

Cell membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei41 – 5919Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini60 – 751692Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. collagen trimer Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 751751Collagen alpha-1(XIII) chain
PRO_0000284680Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi451 – 4511N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9R1N9.

PTM databases

PhosphoSiteiQ9R1N9.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

ArrayExpressiQ9R1N9.
BgeeiQ9R1N9.
CleanExiMM_COL13A1.
GenevestigatoriQ9R1N9.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000090141.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 119119Nonhelical region 1 (NC1)
Add
BLAST
Regioni120 – 223104Triple-helical region 1 (COL1)
Add
BLAST
Regioni224 – 27350Nonhelical region 2 (NC2)
Add
BLAST
Regioni274 – 445172Triple-helical region 2 (COL2)
Add
BLAST
Regioni446 – 46722Nonhelical region 3 (NC3)
Add
BLAST
Regioni468 – 733266Triple-helical region 3 (COL3)
Add
BLAST
Regioni734 – 75118Nonhelical region 4 (NC4)
Add
BLAST

Keywords - Domaini

Collagen, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254293.
GeneTreeiENSGT00750000117303.
HOGENOMiHOG000085653.
HOVERGENiHBG004933.
InParanoidiQ9R1N9.
KOiK16617.
OMAiERQMETA.
PhylomeDBiQ9R1N9.
TreeFamiTF338175.

Family and domain databases

InterProiIPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 7 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms may exist.

Isoform 11 Publication (identifier: Q9R1N9-1) [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

MVAERTRKAA ASGSRGPGEL GAPGPGTVAL AEQCARLPSP GCCGLLALAL    50
CSLALSLLAH FRTAELQARV LRLEAERGEQ QMEKAILGRV NQLLDEKWKF 100
YSRRRREAPK MSPGCNCPPG PPGPTGRPGL PGDKGAIGMP GRVGIKGQPG 150
EKGAPGDAGM SIVGPRGPPG QPGTRGFPGF PGPIGLDGRP GHPGPKGEMG 200
LVGPRGQPGP QGQKGEKGQC GEYPHREYPG GMLAALRSNP IMSLKLLPLL 250
NSVRLAPPPV IKRRTFQGEQ SQTGIQGPPG PPGPPGPSGP LGHPGLPGPI 300
GPPGLPGPPG PKGDPGIQGY HGRKGERGMP GMPGKHGAKG VPGIAVAGMK 350
GEPGTPGTKG EKGAAGSPGL LGQKGEKGDA GNAIGGGRGE PGPPGLPGPP 400
GPKGEAGVDG QAGPPGQQGD KGQPGAAGEQ GPSGPKGAKG EPGKGEMVDY 450
NGSINEALQE IRTLALMGPP GLPGQTGPPG PPGTPGQRGE IGLPGPPGHD 500
GDKGPRGKPG DMGPAGPQGP PGKDGPPGMK GEVGPPGSPG EKGETGQAGP 550
QGLDGPTGEK GEPGDEGRPG ATGLPGPIGL PGFTGEKGEA GEKGDPGAEV 600
PGPPGPEGPP GPPGLQGFPG PKGEAGLEGS KGEKGSQGEK GDRGPLGLPG 650
ASGLDGRPGP PGTPGPIGVP GPAGPKGERG SKGDPGMTGP TGAAGLPGLH 700
GPPGDKGNRG ERGKKGSRGP KGDKGDQGAP GLDAPCPLGE DGLPVQGCWN 750
K 751
Length:751
Mass (Da):73,172
Last modified:May 1, 2000 - v1
Checksum:iFBE2443E1CBF51AD
GO
Isoform 21 Publication (identifier: Q9R1N9-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:739
Mass (Da):72,110
Checksum:iF13951061381F017
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei651 – 66212Missing in isoform 2. 1 Publication
VSP_052388Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30292 mRNA. Translation: AAC24314.1.
AF063693
, 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.
CCDSiCCDS35918.1. [Q9R1N9-2]
RefSeqiNP_031757.1. NM_007731.2. [Q9R1N9-2]
UniGeneiMm.300931.

Genome annotation databases

EnsembliENSMUST00000105454; ENSMUSP00000101094; ENSMUSG00000058806. [Q9R1N9-2]
GeneIDi12817.
KEGGimmu:12817.
UCSCiuc007fgn.1. mouse. [Q9R1N9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30292 mRNA. Translation: AAC24314.1 .
AF063693
, 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 .
CCDSi CCDS35918.1. [Q9R1N9-2 ]
RefSeqi NP_031757.1. NM_007731.2. [Q9R1N9-2 ]
UniGenei Mm.300931.

3D structure databases

ModBasei Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000090141.

PTM databases

PhosphoSitei Q9R1N9.

Proteomic databases

PRIDEi Q9R1N9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000105454 ; ENSMUSP00000101094 ; ENSMUSG00000058806 . [Q9R1N9-2 ]
GeneIDi 12817.
KEGGi mmu:12817.
UCSCi uc007fgn.1. mouse. [Q9R1N9-2 ]

Organism-specific databases

CTDi 1305.
MGIi MGI:1277201. Col13a1.

Phylogenomic databases

eggNOGi NOG254293.
GeneTreei ENSGT00750000117303.
HOGENOMi HOG000085653.
HOVERGENi HBG004933.
InParanoidi Q9R1N9.
KOi K16617.
OMAi ERQMETA.
PhylomeDBi Q9R1N9.
TreeFami TF338175.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

NextBioi 282282.
PROi Q9R1N9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R1N9.
Bgeei Q9R1N9.
CleanExi MM_COL13A1.
Genevestigatori Q9R1N9.

Family and domain databases

InterProi IPR008160. Collagen.
[Graphical view ]
Pfami PF01391. Collagen. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCODA1_MOUSE
AccessioniPrimary (citable) accession number: Q9R1N9
Secondary accession number(s): O70575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 1, 2000
Last modified: September 3, 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

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.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi