CODA1_HUMAN
ID CODA1_HUMAN Reviewed; 717 AA.
AC Q5TAT6; A6NFR5; B9EGD2; E7EWL8; Q13992; Q13993; Q13994; Q13995; Q13996;
AC Q5TAT4; Q5TAT5; Q7KZ33; Q7KZ49; Q99228; Q9NQ52;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Collagen alpha-1(XIII) chain;
DE AltName: Full=COLXIIIA1;
GN Name=COL13A1 {ECO:0000312|HGNC:HGNC:2190};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC00688.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11013208; DOI=10.1093/emboj/19.19.5051;
RA Snellman A., Tu H., Vaisanen T., Kvist A.-P., Huhtala P., Pihlajaniemi T.;
RT "A short sequence in the N-terminal region is required for the
RT trimerization of type XIII collagen and is conserved in other collagenous
RT transmembrane proteins.";
RL EMBO J. 19:5051-5059(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAA51685.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-717 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 84-717 (ISOFORMS 8 AND 9).
RC TISSUE=Endothelial cell {ECO:0000312|EMBL:AAA51685.1};
RX PubMed=1698771; DOI=10.1016/s0021-9258(17)44849-6;
RA Pihlajaniemi T., Tamminen M.;
RT "The alpha 1 chain of type XIII collagen consists of three collagenous and
RT four noncollagenous domains, and its primary transcript undergoes complex
RT alternative splicing.";
RL J. Biol. Chem. 265:16922-16928(1990).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAA52047.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 457-717 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 573-717 (ISOFORMS 3/4/7/8).
RC TISSUE=Fibrosarcoma {ECO:0000312|EMBL:AAA52047.1};
RX PubMed=3547403; DOI=10.1073/pnas.84.4.940;
RA Pihlajaniemi T., Myllyla R., Seyer J., Kurkinen M., Prockop D.J.;
RT "Partial characterization of a low molecular weight human collagen that
RT undergoes alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:940-944(1987).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAA51987.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 551-717 (ISOFORMS 6 AND 7), NUCLEOTIDE
RP SEQUENCE [GENOMIC DNA] OF 551-717 (ISOFORMS 1/2), AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 566-771 (ISOFORMS 3/4/8).
RX PubMed=2459707; DOI=10.1073/pnas.85.20.7491;
RA Tikka L., Pihlajaniemi T., Henttu P., Prockop D.J., Tryggvason K.;
RT "Gene structure for the alpha 1 chain of a human short-chain collagen (type
RT XIII) with alternatively spliced transcripts and translation termination
RT codon at the 5' end of the last exon.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7491-7495(1988).
RN [7] {ECO:0000305}
RP ALTERNATIVE SPLICING.
RX PubMed=1447209; DOI=10.1016/s0021-9258(18)35820-4;
RA Juvonen M., Pihlajaniemi T.;
RT "Characterization of the spectrum of alternative splicing of alpha 1 (XIII)
RT collagen transcripts in HT-1080 cells and calvarial tissue resulted in
RT identification of two previously unidentified alternatively spliced
RT sequences, one previously unidentified exon, and nine new mRNA variants.";
RL J. Biol. Chem. 267:24693-24699(1992).
RN [8] {ECO:0000305}
RP ALTERNATIVE SPLICING.
RX PubMed=1447210; DOI=10.1016/s0021-9258(18)35821-6;
RA Juvonen M., Sandberg M., Pihlajaniemi T.;
RT "Patterns of expression of the six alternatively spliced exons affecting
RT the structures of the COL1 and NC2 domains of the alpha 1(XIII) collagen
RT chain in human tissues and cell lines.";
RL J. Biol. Chem. 267:24700-24707(1992).
RN [9] {ECO:0000305}
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=8246446;
RA Juvonen M., Pihlajaniemi T., Autio-Harmainen H.;
RT "Location and alternative splicing of type XIII collagen RNA in the early
RT human placenta.";
RL Lab. Invest. 69:541-551(1993).
RN [10] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10865988; DOI=10.1006/exer.1998.0826;
RA Sandberg-Lall M., Hagg P.O., Wahlstrom I., Pihlajaniemi T.;
RT "Type XIII collagen is widely expressed in the adult and developing human
RT eye and accentuated in the ciliary muscle, the optic nerve and the neural
RT retina.";
RL Exp. Eye Res. 70:401-410(2000).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FN1; HSPG2 AND NID2, AND HEPARIN-BINDING.
RX PubMed=11956183; DOI=10.1074/jbc.m107583200;
RA Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R.,
RA Pihlajaniemi T.;
RT "The type XIII collagen ectodomain is a 150-nm rod and capable of binding
RT to fibronectin, nidogen-2, perlecan, and heparin.";
RL J. Biol. Chem. 277:23092-23099(2002).
RN [12]
RP INVOLVEMENT IN CMS19, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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:Q9R1N9, ECO:0000269|PubMed:10865988,
CC ECO:0000269|PubMed:11956183, 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.
CC {ECO:0000269|PubMed:11013208, ECO:0000269|PubMed:11956183}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11013208};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:11013208}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:26626625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1 {ECO:0000269|PubMed:11013208};
CC IsoId=Q5TAT6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15164054};
CC IsoId=Q5TAT6-2; Sequence=VSP_052383;
CC Name=3 {ECO:0000269|PubMed:15164054};
CC IsoId=Q5TAT6-3; Sequence=VSP_052383, VSP_052386;
CC Name=4 {ECO:0000269|PubMed:1698771};
CC IsoId=Q5TAT6-4; Sequence=VSP_052383, VSP_052384, VSP_052386;
CC Name=5 {ECO:0000269|PubMed:3547403};
CC IsoId=Q5TAT6-5; Sequence=VSP_052384;
CC Name=6 {ECO:0000269|PubMed:2459707};
CC IsoId=Q5TAT6-6; Sequence=VSP_052385;
CC Name=7 {ECO:0000269|PubMed:2459707};
CC IsoId=Q5TAT6-7; Sequence=VSP_052385, VSP_052386;
CC Name=8 {ECO:0000269|PubMed:1698771};
CC IsoId=Q5TAT6-8; Sequence=VSP_052382, VSP_052386;
CC Name=9 {ECO:0000269|PubMed:1698771};
CC IsoId=Q5TAT6-9; Sequence=VSP_052383, VSP_052384, VSP_052386,
CC VSP_052387;
CC Name=10;
CC IsoId=Q5TAT6-10; Sequence=VSP_043361, VSP_052382, VSP_052384;
CC Name=11;
CC IsoId=Q5TAT6-11; Sequence=VSP_047230, VSP_052383, VSP_052384,
CC VSP_052386, VSP_047231;
CC -!- TISSUE SPECIFICITY: Widely expressed in both fetal and adult ocular
CC tissues (at protein level). In the eye, expression is accentuated in
CC the ciliary muscle, optic nerve and the neural retina. In early
CC placenta, localized to fibroblastoid stromal cells of the placental
CC villi, to endothelial cells of developing capillaries and to cells of
CC the cytotrophoblastic columns. Also detected in large decidual cells of
CC the decidual membrane and to stromal cells of the gestational
CC endometrium, but not in the epithelial cells in the endometrial glands.
CC Isoform 10: Expressed in muscle (PubMed:26626625).
CC {ECO:0000269|PubMed:10865988, ECO:0000269|PubMed:26626625,
CC ECO:0000269|PubMed:8246446}.
CC -!- DISEASE: Myasthenic syndrome, congenital, 19 (CMS19) [MIM:616720]: A
CC form of congenital myasthenic syndrome, a group of disorders
CC characterized by failure of neuromuscular transmission, including pre-
CC synaptic, synaptic, and post-synaptic disorders that are not of
CC autoimmune origin. Clinical features are easy fatigability and muscle
CC weakness affecting the axial and limb muscles (with hypotonia in early-
CC onset forms), the ocular muscles (leading to ptosis and
CC ophthalmoplegia), and the facial and bulbar musculature (affecting
CC sucking and swallowing, and leading to dysphonia). The symptoms
CC fluctuate and worsen with physical effort.
CC {ECO:0000269|PubMed:26626625}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51685.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ293624; CAC00688.1; -; mRNA.
DR EMBL; AC024601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136385; AAI36386.1; -; mRNA.
DR EMBL; M59217; AAA51685.1; ALT_INIT; mRNA.
DR EMBL; M33653; AAA52047.1; -; mRNA.
DR EMBL; M15524; AAA52048.1; -; mRNA.
DR EMBL; M20803; AAA51987.1; -; Genomic_DNA.
DR EMBL; M20795; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20796; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20797; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20798; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20799; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20800; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20801; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20802; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20804; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20805; AAA51987.1; JOINED; Genomic_DNA.
DR EMBL; M20803; AAA51988.1; -; Genomic_DNA.
DR EMBL; M20795; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20796; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20797; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20798; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20799; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20800; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20801; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20802; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20804; AAA51988.1; JOINED; Genomic_DNA.
DR EMBL; M20803; AAA51989.1; -; Genomic_DNA.
DR EMBL; M20795; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20796; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20797; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20798; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20799; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20801; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20802; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20804; AAA51989.1; JOINED; Genomic_DNA.
DR EMBL; M20803; AAA51990.1; -; Genomic_DNA.
DR EMBL; M20796; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20797; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20798; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20799; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20800; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20801; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20802; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20804; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20805; AAA51990.1; JOINED; Genomic_DNA.
DR EMBL; M20803; AAA51991.1; -; Genomic_DNA.
DR EMBL; M20796; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20797; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20798; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20799; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20801; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20802; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20804; AAA51991.1; JOINED; Genomic_DNA.
DR EMBL; M20805; AAA51991.1; JOINED; Genomic_DNA.
DR CCDS; CCDS44419.1; -. [Q5TAT6-1]
DR CCDS; CCDS44423.2; -. [Q5TAT6-4]
DR CCDS; CCDS44424.2; -. [Q5TAT6-2]
DR CCDS; CCDS44425.2; -. [Q5TAT6-8]
DR CCDS; CCDS44427.2; -. [Q5TAT6-10]
DR CCDS; CCDS44428.2; -. [Q5TAT6-11]
DR PIR; B40983; B40983.
DR RefSeq; NP_001123575.1; NM_001130103.1. [Q5TAT6-1]
DR RefSeq; NP_542988.3; NM_080798.3. [Q5TAT6-10]
DR RefSeq; NP_542990.3; NM_080800.3. [Q5TAT6-8]
DR RefSeq; NP_542991.3; NM_080801.3. [Q5TAT6-2]
DR RefSeq; NP_542992.3; NM_080802.3. [Q5TAT6-4]
DR RefSeq; NP_542995.3; NM_080805.3. [Q5TAT6-11]
DR AlphaFoldDB; Q5TAT6; -.
DR BioGRID; 107701; 10.
DR ComplexPortal; CPX-1754; Collagen type XIII trimer.
DR IntAct; Q5TAT6; 1.
DR STRING; 9606.ENSP00000381949; -.
DR iPTMnet; Q5TAT6; -.
DR PhosphoSitePlus; Q5TAT6; -.
DR BioMuta; COL13A1; -.
DR DMDM; 74745860; -.
DR jPOST; Q5TAT6; -.
DR MassIVE; Q5TAT6; -.
DR PaxDb; Q5TAT6; -.
DR PeptideAtlas; Q5TAT6; -.
DR PRIDE; Q5TAT6; -.
DR ProteomicsDB; 18870; -.
DR ProteomicsDB; 64863; -. [Q5TAT6-1]
DR ProteomicsDB; 64864; -. [Q5TAT6-10]
DR ProteomicsDB; 64865; -. [Q5TAT6-2]
DR ProteomicsDB; 64866; -. [Q5TAT6-3]
DR ProteomicsDB; 64867; -. [Q5TAT6-4]
DR ProteomicsDB; 64868; -. [Q5TAT6-5]
DR ProteomicsDB; 64869; -. [Q5TAT6-6]
DR ProteomicsDB; 64870; -. [Q5TAT6-7]
DR ProteomicsDB; 64871; -. [Q5TAT6-8]
DR ProteomicsDB; 64872; -. [Q5TAT6-9]
DR Antibodypedia; 28918; 103 antibodies from 26 providers.
DR DNASU; 1305; -.
DR Ensembl; ENST00000354547.7; ENSP00000346553.3; ENSG00000197467.17. [Q5TAT6-2]
DR Ensembl; ENST00000398978.8; ENSP00000381949.3; ENSG00000197467.17. [Q5TAT6-1]
DR Ensembl; ENST00000517713.5; ENSP00000430061.1; ENSG00000197467.17. [Q5TAT6-4]
DR Ensembl; ENST00000520133.5; ENSP00000430173.1; ENSG00000197467.17. [Q5TAT6-11]
DR Ensembl; ENST00000520267.5; ENSP00000428057.1; ENSG00000197467.17. [Q5TAT6-10]
DR Ensembl; ENST00000522165.5; ENSP00000428342.1; ENSG00000197467.17. [Q5TAT6-8]
DR GeneID; 1305; -.
DR KEGG; hsa:1305; -.
DR UCSC; uc057tuj.1; human. [Q5TAT6-1]
DR CTD; 1305; -.
DR DisGeNET; 1305; -.
DR GeneCards; COL13A1; -.
DR HGNC; HGNC:2190; COL13A1.
DR HPA; ENSG00000197467; Tissue enhanced (epididymis).
DR MalaCards; COL13A1; -.
DR MIM; 120350; gene.
DR MIM; 616720; phenotype.
DR neXtProt; NX_Q5TAT6; -.
DR OpenTargets; ENSG00000197467; -.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA26706; -.
DR VEuPathDB; HostDB:ENSG00000197467; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154865; -.
DR HOGENOM; CLU_020867_0_0_1; -.
DR InParanoid; Q5TAT6; -.
DR OrthoDB; 669310at2759; -.
DR PhylomeDB; Q5TAT6; -.
DR TreeFam; TF338175; -.
DR PathwayCommons; Q5TAT6; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q5TAT6; -.
DR BioGRID-ORCS; 1305; 8 hits in 1063 CRISPR screens.
DR ChiTaRS; COL13A1; human.
DR GeneWiki; Collagen,_type_XIII,_alpha_1; -.
DR GenomeRNAi; 1305; -.
DR Pharos; Q5TAT6; Tbio.
DR PRO; PR:Q5TAT6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5TAT6; protein.
DR Bgee; ENSG00000197467; Expressed in cerebellar hemisphere and 149 other tissues.
DR ExpressionAtlas; Q5TAT6; baseline and differential.
DR Genevisible; Q5TAT6; HS.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0005600; C:collagen type XIII trimer; TAS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IEP:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IPI:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001763; P:morphogenesis of a branching structure; ISS: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; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Collagen;
KW Congenital myasthenic syndrome; Developmental protein; Differentiation;
KW Disulfide bond; Heparin-binding; Membrane; Osteogenesis;
KW Postsynaptic cell membrane; Reference proteome; Signal-anchor; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..717
FT /note="Collagen alpha-1(XIII) chain"
FT /id="PRO_0000284679"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..61
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..121
FT /note="Nonhelical region 1 (NC1)"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..216
FT /note="Triple-helical region 1 (COL1)"
FT /evidence="ECO:0000255"
FT REGION 217..269
FT /note="Nonhelical region 2 (NC2)"
FT /evidence="ECO:0000255"
FT REGION 259..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..441
FT /note="Triple-helical region 2 (COL2)"
FT /evidence="ECO:0000255"
FT REGION 442..463
FT /note="Nonhelical region 3 (NC3)"
FT /evidence="ECO:0000255"
FT REGION 463..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..699
FT /note="Triple-helical region 3 (COL3)"
FT /evidence="ECO:0000255"
FT REGION 700..717
FT /note="Nonhelical region 4 (NC4)"
FT /evidence="ECO:0000255"
FT COMPBIAS 116..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 122..159
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043361"
FT VAR_SEQ 135..163
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_047230"
FT VAR_SEQ 220..238
FT /note="Missing (in isoform 8 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1698771"
FT /id="VSP_052382"
FT VAR_SEQ 239..260
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:1698771"
FT /id="VSP_052383"
FT VAR_SEQ 551..565
FT /note="Missing (in isoform 4, isoform 5, isoform 9, isoform
FT 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1698771, ECO:0000303|PubMed:3547403"
FT /id="VSP_052384"
FT VAR_SEQ 566..579
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:2459707"
FT /id="VSP_052385"
FT VAR_SEQ 617..628
FT /note="Missing (in isoform 3, isoform 4, isoform 7, isoform
FT 8, isoform 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:1698771"
FT /id="VSP_052386"
FT VAR_SEQ 676..705
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:1698771"
FT /id="VSP_052387"
FT VAR_SEQ 678..706
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_047231"
FT VARIANT 531
FT /note="H -> Q (in dbSNP:rs1061954)"
FT /id="VAR_055670"
FT CONFLICT 182
FT /note="K -> F (in Ref. 4; AAA51685)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="G -> A (in Ref. 1; CAC00688 and 4; AAA51685)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 480..481
FT /note="IP -> ML (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="Missing (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="P -> L (in Ref. 4; AAA51685 and 5; AAA52047)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="P -> L (in Ref. 5; AAA52047 and 6; AAA51987/
FT AAA51990/AAA51991)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="E -> Q (in Ref. 5; AAA52047/AAA52048 and 6;
FT AAA51987/AAA51988/AAA51989/AAA51990/AAA51991)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="L -> Y (in Ref. 6; AAA51987/AAA51988/AAA51989/
FT AAA51990/AAA51991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 69950 MW; FD12CA80CC93540F CRC64;
MVAERTHKAA ATGARGPGEL GAPGTVALVA ARAERGARLP SPGSCGLLTL ALCSLALSLL
AHFRTAELQA RVLRLEAERG EQQMETAILG RVNQLLDEKW KLHSRRRREA PKTSPGCNCP
PGPPGPTGRP GLPGDKGAIG MPGRVGSPGD AGLSIIGPRG PPGQPGTRGF PGFPGPIGLD
GKPGHPGPKG DMGLTGPPGQ PGPQGQKGEK GQCGEYPHRE CLSSMPAALR SSQIIALKLL
PLLNSVRLAP PPVIKRRTFQ GEQSQASIQG PPGPPGPPGP SGPLGHPGLP GPMGPPGLPG
PPGPKGDPGI QGYHGRKGER GMPGMPGKHG AKGAPGIAVA GMKGEPGIPG TKGEKGAEGS
PGLPGLLGQK GEKGDAGNSI GGGRGEPGPP GLPGPPGPKG EAGVDGQVGP PGQPGDKGER
GAAGEQGPDG PKGSKGEPGK GEMVDYNGNI NEALQEIRTL ALMGPPGLPG QIGPPGAPGI
PGQKGEIGLP GPPGHDGEKG PRGKPGDMGP PGPQGPPGKD GPPGVKGENG HPGSPGEKGE
KGETGQAGSP GEKGEAGEKG NPGAEVPGLP GPEGPPGPPG LQGVPGPKGE AGLDGAKGEK
GFQGEKGDRG PLGLPGASGL DGRPGPPGTP GPIGVPGPAG PKGERGSKGD PGMTGPTGAA
GLPGLHGPPG DKGNRGERGK KGSRGPKGDK GDQGAPGLDA PCPLGEDGLP VQGCWNK
