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 27-MAR-2024, entry version 157. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 12. DR ComplexPortal; CPX-1754; Collagen type XIII trimer. DR IntAct; Q5TAT6; 1. DR STRING; 9606.ENSP00000381949; -. DR iPTMnet; Q5TAT6; -. DR PhosphoSitePlus; Q5TAT6; -. DR SwissPalm; Q5TAT6; -. DR BioMuta; COL13A1; -. DR DMDM; 74745860; -. DR jPOST; Q5TAT6; -. DR MassIVE; Q5TAT6; -. DR PaxDb; 9606-ENSP00000381949; -. DR PeptideAtlas; 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; 112 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 AGR; HGNC:2190; -. DR CTD; 1305; -. DR DisGeNET; 1305; -. DR GeneCards; COL13A1; -. DR HGNC; HGNC:2190; COL13A1. DR HPA; ENSG00000197467; Tissue enhanced (brain, 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; 4271163at2759; -. 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 1141 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 151 other cell types or tissues. DR ExpressionAtlas; Q5TAT6; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; 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: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:0030020; F:extracellular matrix structural constituent conferring tensile strength; 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: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:0001501; P:skeletal system development; IBA:GO_Central. DR InterPro; IPR008160; Collagen. DR PANTHER; PTHR37456:SF4; COLLAGEN ALPHA-1(XIII) CHAIN ISOFORM X2; 1. DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1. DR Pfam; PF01391; Collagen; 9. DR Genevisible; Q5TAT6; HS. 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; FT AAA51987/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; FT AAA51987/AAA51988/AAA51989/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 //