CODA1_MOUSE
ID CODA1_MOUSE Reviewed; 751 AA.
AC Q9R1N9; O70575;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Collagen alpha-1(XIII) chain;
GN Name=Col13a1 {ECO:0000312|MGI:MGI:1277201};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC24314.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Intestine;
RX PubMed=9624150; DOI=10.1074/jbc.273.25.15590;
RA Hagg P., Rehn M., Huhtala P., Vaisanen T., Tamminen M., Pihlajaniemi T.;
RT "Type XIII collagen is identified as a plasma membrane protein.";
RL J. Biol. Chem. 273:15590-15597(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD50327.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=10429945; DOI=10.1016/s0945-053x(99)00018-9;
RA Kvist A.-P., Latvanlehto A., Sund M., Horelli-Kuitunen N., Rehn M.,
RA Palotie A., Beier D., Pihlajaniemi T.;
RT "Complete exon-intron organization and chromosomal location of the gene for
RT mouse type XIII collagen (col13a1) and comparison with its human
RT homologue.";
RL Matrix Biol. 18:261-274(1999).
RN [3] {ECO:0000305}
RP FUNCTION, AND TRANSGENIC MICE.
RX PubMed=11583983; DOI=10.1016/s0002-9440(10)62542-4;
RA Kvist A.-P., Latvanlehto A., Sund M., Eklund L., Vaisanen T., Hagg P.,
RA Sormunen R., Komulainen J., Fassler R., Pihlajaniemi T.;
RT "Lack of cytosolic and transmembrane domains of type XIII collagen results
RT in progressive myopathy.";
RL Am. J. Pathol. 159:1581-1592(2001).
RN [4] {ECO:0000305}
RP FUNCTION, AND TRANSGENIC MICE.
RX PubMed=11566879; DOI=10.1093/emboj/20.18.5153;
RA Sund M., Ylonen R., Tuomisto A., Sormunen R., Tahkola J., Kvist A.-P.,
RA Kontusaari S., Autio-Harmainen H., Pihlajaniemi T.;
RT "Abnormal adherence junctions in the heart and reduced angiogenesis in
RT transgenic mice overexpressing mutant type XIII collagen.";
RL EMBO J. 20:5153-5164(2001).
RN [5] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=11470398; DOI=10.1016/s0945-053x(01)00134-2;
RA Sund M., Vaisanen T., Kaukinen S., Ilves M., Tu H., Autio-Harmainen H.,
RA Rauvala H., Pihlajaniemi T.;
RT "Distinct expression of type XIII collagen in neuronal structures and other
RT tissues during mouse development.";
RL Matrix Biol. 20:215-231(2001).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=16007336; DOI=10.1359/jbmr.050319;
RA Ylonen R., Kyronlahti T., Sund M., Ilves M., Lehenkari P., Tuukkanen J.,
RA Pihlajaniemi T.;
RT "Type XIII collagen strongly affects bone formation in transgenic mice.";
RL J. Bone Miner. Res. 20:1381-1393(2005).
RN [7]
RP FUNCTION.
RX PubMed=26626625; DOI=10.1016/j.ajhg.2015.10.017;
RA Logan C.V., Cossins J., Rodriguez Cruz P.M., Parry D.A., Maxwell S.,
RA Martinez-Martinez P., Riepsaame J., Abdelhamed Z.A., Lake A.V., Moran M.,
RA Robb S., Chow G., Sewry C., Hopkins P.M., Sheridan E., Jayawant S.,
RA Palace J., Johnson C.A., Beeson D.;
RT "Congenital myasthenic syndrome type 19 is caused by mutations in COL13A1,
RT Encoding the atypical non-fibrillar collagen type XIII alpha1 chain.";
RL Am. J. Hum. Genet. 97:878-885(2015).
CC -!- FUNCTION: Involved in cell-matrix and cell-cell adhesion interactions
CC that are required for normal development. May participate in the
CC linkage between muscle fiber and basement membrane. May play a role in
CC endochondral ossification of bone and branching morphogenesis of lung.
CC Binds heparin. At neuromuscular junctions, may play a role in
CC acetylcholine receptor clustering (PubMed:26626625).
CC {ECO:0000250|UniProtKB:Q5TAT6, ECO:0000269|PubMed:11566879,
CC ECO:0000269|PubMed:11583983, ECO:0000269|PubMed:16007336,
CC ECO:0000269|PubMed:26626625}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Nucleation of the type XIII
CC collagen triple helix is likely to occur at the N-terminal region with
CC triple helix formation proceeding from the N- to the C-terminus.
CC Interacts with FN1, perlecan/HSPG2 and NID2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9624150};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9624150}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q5TAT6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist. {ECO:0000305};
CC Name=1 {ECO:0000269|PubMed:10429945};
CC IsoId=Q9R1N9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9624150};
CC IsoId=Q9R1N9-2; Sequence=VSP_052388;
CC -!- DEVELOPMENTAL STAGE: Expression levels remain fairly constant during
CC early fetal development. This is followed by a marked increase of
CC expression levels during the final stages of organogenesis, with
CC initiation of the rapid fetal growth phase before birth. At mid-
CC gestation, strongly expressed in the central and peripheral nervous
CC systems. Also strongly expressed in developing heart, with localization
CC to cell-cell contacts and accentuated in intercalated disks
CC perinatally. During late fetal development, expressed in many tissues
CC including cartilage, bone, skeletal muscle, lung, intestine and skin.
CC Not detected in endothelia of most blood vessels or the endocardium of
CC the heart. {ECO:0000269|PubMed:11470398}.
CC -!- MISCELLANEOUS: Transgenic mice overexpressing COL13A1 with a 90 amino
CC acid in-frame deletion of the COL2 sequence show embryonic lethality
CC due either to a lack of placental formation or to cardiovascular
CC defects in offspring from heterozygous mating. In contrast, transgenic
CC mice expressing an N-terminally altered COL13A1 lacking both cytosolic
CC and transmembrane domains while retaining the collagenous ectodomain
CC are viable and fertile, but display progressive muscular myopathy.
CC {ECO:0000269|PubMed:11566879, ECO:0000269|PubMed:11583983}.
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DR EMBL; U30292; AAC24314.1; -; mRNA.
DR EMBL; AF063693; AAD50327.1; -; Genomic_DNA.
DR EMBL; AF063666; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063667; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063668; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063669; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063670; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063671; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063672; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063673; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063674; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063675; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063676; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063677; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063678; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063679; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063680; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063681; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063682; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063683; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063684; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063685; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063686; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063687; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063688; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063689; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063690; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063691; AAD50327.1; JOINED; Genomic_DNA.
DR EMBL; AF063692; AAD50327.1; JOINED; Genomic_DNA.
DR CCDS; CCDS35918.1; -. [Q9R1N9-2]
DR RefSeq; NP_031757.1; NM_007731.3. [Q9R1N9-2]
DR AlphaFoldDB; Q9R1N9; -.
DR ComplexPortal; CPX-2980; Collagen type XIII trimer.
DR STRING; 10090.ENSMUSP00000101094; -.
DR GlyGen; Q9R1N9; 1 site.
DR iPTMnet; Q9R1N9; -.
DR PhosphoSitePlus; Q9R1N9; -.
DR MaxQB; Q9R1N9; -.
DR PaxDb; Q9R1N9; -.
DR PRIDE; Q9R1N9; -.
DR ProteomicsDB; 283599; -. [Q9R1N9-1]
DR ProteomicsDB; 283600; -. [Q9R1N9-2]
DR Antibodypedia; 28918; 103 antibodies from 26 providers.
DR DNASU; 12817; -.
DR Ensembl; ENSMUST00000105454; ENSMUSP00000101094; ENSMUSG00000058806. [Q9R1N9-2]
DR GeneID; 12817; -.
DR KEGG; mmu:12817; -.
DR UCSC; uc007fgn.2; mouse. [Q9R1N9-2]
DR CTD; 1305; -.
DR MGI; MGI:1277201; Col13a1.
DR VEuPathDB; HostDB:ENSMUSG00000058806; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154865; -.
DR InParanoid; Q9R1N9; -.
DR OMA; XGASGLD; -.
DR OrthoDB; 669310at2759; -.
DR PhylomeDB; Q9R1N9; -.
DR TreeFam; TF338175; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12817; 0 hits in 61 CRISPR screens.
DR PRO; PR:Q9R1N9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9R1N9; protein.
DR Bgee; ENSMUSG00000058806; Expressed in Meckel's cartilage and 167 other tissues.
DR ExpressionAtlas; Q9R1N9; baseline and differential.
DR Genevisible; Q9R1N9; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0001958; P:endochondral ossification; IEP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IEP:UniProtKB.
DR GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Collagen;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Heparin-binding; Membrane; Osteogenesis; Postsynaptic cell membrane;
KW Reference proteome; Signal-anchor; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..751
FT /note="Collagen alpha-1(XIII) chain"
FT /id="PRO_0000284680"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..119
FT /note="Nonhelical region 1 (NC1)"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..223
FT /note="Triple-helical region 1 (COL1)"
FT /evidence="ECO:0000255"
FT REGION 190..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..273
FT /note="Nonhelical region 2 (NC2)"
FT /evidence="ECO:0000255"
FT REGION 265..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..445
FT /note="Triple-helical region 2 (COL2)"
FT /evidence="ECO:0000255"
FT REGION 446..467
FT /note="Nonhelical region 3 (NC3)"
FT /evidence="ECO:0000255"
FT REGION 466..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..733
FT /note="Triple-helical region 3 (COL3)"
FT /evidence="ECO:0000255"
FT REGION 734..751
FT /note="Nonhelical region 4 (NC4)"
FT /evidence="ECO:0000255"
FT COMPBIAS 277..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 651..662
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9624150"
FT /id="VSP_052388"
SQ SEQUENCE 751 AA; 73172 MW; FBE2443E1CBF51AD CRC64;
MVAERTRKAA ASGSRGPGEL GAPGPGTVAL AEQCARLPSP GCCGLLALAL CSLALSLLAH
FRTAELQARV LRLEAERGEQ QMEKAILGRV NQLLDEKWKF YSRRRREAPK MSPGCNCPPG
PPGPTGRPGL PGDKGAIGMP GRVGIKGQPG EKGAPGDAGM SIVGPRGPPG QPGTRGFPGF
PGPIGLDGRP GHPGPKGEMG LVGPRGQPGP QGQKGEKGQC GEYPHREYPG GMLAALRSNP
IMSLKLLPLL NSVRLAPPPV IKRRTFQGEQ SQTGIQGPPG PPGPPGPSGP LGHPGLPGPI
GPPGLPGPPG PKGDPGIQGY HGRKGERGMP GMPGKHGAKG VPGIAVAGMK GEPGTPGTKG
EKGAAGSPGL LGQKGEKGDA GNAIGGGRGE PGPPGLPGPP GPKGEAGVDG QAGPPGQQGD
KGQPGAAGEQ GPSGPKGAKG EPGKGEMVDY NGSINEALQE IRTLALMGPP GLPGQTGPPG
PPGTPGQRGE IGLPGPPGHD GDKGPRGKPG DMGPAGPQGP PGKDGPPGMK GEVGPPGSPG
EKGETGQAGP QGLDGPTGEK GEPGDEGRPG ATGLPGPIGL PGFTGEKGEA GEKGDPGAEV
PGPPGPEGPP GPPGLQGFPG PKGEAGLEGS KGEKGSQGEK GDRGPLGLPG ASGLDGRPGP
PGTPGPIGVP GPAGPKGERG SKGDPGMTGP TGAAGLPGLH GPPGDKGNRG ERGKKGSRGP
KGDKGDQGAP GLDAPCPLGE DGLPVQGCWN K
