ID COBA1_HUMAN Reviewed; 1806 AA. AC P12107; B1ASK7; D3DT73; E9PCU0; Q14034; Q149N0; Q9UIT4; Q9UIT5; Q9UIT6; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 27-MAR-2024, entry version 238. DE RecName: Full=Collagen alpha-1(XI) chain; DE Flags: Precursor; GN Name=COL11A1; Synonyms=COLL6; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANTS LEU-1323 AND PRO-1535. RX PubMed=1690726; DOI=10.1016/s0021-9258(19)39343-3; RA Yoshioka H., Ramirez F.; RT "Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and RT expression of the gene in tumor cell lines."; RL J. Biol. Chem. 265:6423-6426(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B AND RP C), AND VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926 DEL; RP 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535. RX PubMed=10486316; DOI=10.1086/302585; RA Annunen S., Koerkkoe J., Czarny M., Warman M.L., Brunner H.G., RA Kaeaeriaeinen H., Mulliken J.B., Tranebjaerg L., Brooks D.G., Cox G.F., RA Cruysberg J.R., Curtis M.A., Davenport S.L.H., Friedrich C.A., Kaitila I., RA Krawczynski M.R., Latos-Bielenska A., Mukai S., Olsen B.R., Shinno N., RA Somer M., Vikkula M., Zlotogora J., Prockop D.J., Ala-Kokko L.; RT "Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall RT syndrome, but other mutations cause overlapping Marshall/Stickler RT phenotypes."; RL Am. J. Hum. Genet. 65:974-983(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-1535. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS LEU-1323 RP AND PRO-1535. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 538-1806, PARTIAL PROTEIN SEQUENCE, AND RP ALLYSINE AT LYS-612 AND LYS-1452. RX PubMed=3182841; DOI=10.1016/s0021-9258(18)37512-4; RA Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T., RA Ninomiya Y., Olsen B.R., Ramirez F.; RT "Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that RT type XI belongs to the fibrillar class of collagens and reveals that the RT expression of the gene is not restricted to cartilagenous tissue."; RL J. Biol. Chem. 263:17159-17166(1988). RN [7] RP ALTERNATIVE SPLICING. RC TISSUE=Blood; RX PubMed=7721876; DOI=10.1074/jbc.270.16.9486; RA Zhidkova N.I., Justice S.K., Mayne R.; RT "Alternative mRNA processing occurs in the variable region of the pro-alpha RT 1(XI) and pro-alpha 2(XI) collagen chains."; RL J. Biol. Chem. 270:9486-9493(1995). RN [8] RP INVOLVEMENT IN DFNA37. RX PubMed=30245514; DOI=10.1038/s41436-018-0285-0; RA Booth K.T., Askew J.W., Talebizadeh Z., Huygen P.L.M., Eudy J., Kenyon J., RA Hoover D., Hildebrand M.S., Smith K.R., Bahlo M., Kimberling W.J., RA Smith R.J.H., Azaiez H., Smith S.D.; RT "Splice-altering variant in COL11A1 as a cause of nonsyndromic hearing loss RT DFNA37."; RL Genet. Med. 21:948-954(2019). RN [9] RP VARIANT STL2 VAL-625. RX PubMed=8872475; DOI=10.1093/hmg/5.9.1339; RA Richards A.J., Yates J.R.W., Williams R., Payne S.J., Pope F.M., RA Scott J.D., Snead M.P.; RT "A family with Stickler syndrome type 2 has a mutation in the COL11A1 gene RT resulting in the substitution of glycine 97 by valine in alpha-1(XI) RT collagen."; RL Hum. Mol. Genet. 5:1339-1343(1996). RN [10] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-1326; LYS-1328 AND LEU-1328. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [11] RP VARIANTS FBCG1 ARG-796 AND ARG-1042. RX PubMed=21035103; DOI=10.1016/j.ajhg.2010.10.009; RA Tompson S.W., Bacino C.A., Safina N.P., Bober M.B., Proud V.K., Funari T., RA Wangler M.F., Nevarez L., Ala-Kokko L., Wilcox W.R., Eyre D.R., Krakow D., RA Cohn D.H.; RT "Fibrochondrogenesis results from mutations in the COL11A1 type XI collagen RT gene."; RL Am. J. Hum. Genet. 87:708-712(2010). RN [12] RP VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND RP VAL-1516. RX PubMed=20513134; DOI=10.1002/humu.21257; RA Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S., RA Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.; RT "Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and RT COL11A1."; RL Hum. Mutat. 31:E1461-E1471(2010). CC -!- FUNCTION: May play an important role in fibrillogenesis by controlling CC lateral growth of collagen II fibrils. CC -!- SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha CC 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational CC modification of alpha 1(II). Alpha 1(V) can also be found instead of CC alpha 3(XI)=1(II). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist. There is alternative usage CC of exon IIA or exon IIB. Transcripts containing exon IIA or IIB are CC present in cartilage, but exon IIB is preferentially utilized in CC transcripts from tendon.; CC Name=A; CC IsoId=P12107-1; Sequence=Displayed; CC Name=B; CC IsoId=P12107-2; Sequence=VSP_001145; CC Name=C; CC IsoId=P12107-3; Sequence=VSP_001146; CC Name=4; CC IsoId=P12107-4; Sequence=VSP_046318; CC -!- TISSUE SPECIFICITY: Cartilage, placenta and some tumor or virally CC transformed cell lines. Isoforms using exon IIA or IIB are found in the CC cartilage while isoforms using only exon IIB are found in the tendon. CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have CC crucial roles in tissue growth and repair by controlling both the CC intracellular assembly of procollagen molecules and the extracellular CC assembly of collagen fibrils. It binds a calcium ion which is essential CC for its function (By similarity). {ECO:0000250}. CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- DISEASE: Stickler syndrome 2 (STL2) [MIM:604841]: An autosomal dominant CC form of Stickler syndrome, an inherited disorder that associates ocular CC signs with more or less complete forms of Pierre Robin sequence, bone CC disorders and sensorineural deafness. Ocular disorders may include CC juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal CC degeneration, retinal detachment, and chronic uveitis. Pierre Robin CC sequence includes an opening in the roof of the mouth (a cleft palate), CC a large tongue (macroglossia), and a small lower jaw (micrognathia). CC Bones are affected by slight platyspondylisis and large, often CC defective epiphyses. Juvenile joint laxity is followed by early signs CC of arthrosis. The degree of hearing loss varies among affected CC individuals and may become more severe over time. Syndrome expressivity CC is variable. {ECO:0000269|PubMed:10486316, ECO:0000269|PubMed:20513134, CC ECO:0000269|PubMed:8872475}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Marshall syndrome (MRSHS) [MIM:154780]: An autosomal dominant CC disorder characterized by ocular abnormalities, deafness, craniofacial CC anomalies, and anhidrotic ectodermal dysplasia. Clinical features CC include short stature; flat or retruded midface with short, depressed CC nose, flat nasal bridge and anteverted nares; cleft palate with or CC without the Pierre Robin sequence; appearance of large eyes with ocular CC hypertelorism; cataracts, either congenital or juvenile; esotropia; CC high myopia; sensorineural hearing loss; spondyloepiphyseal CC abnormalities; calcification of the falx cerebri; ectodermal CC abnormalities, including defects in sweating and dental structures. CC {ECO:0000269|PubMed:10486316}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe short- CC limbed skeletal dysplasia characterized by broad long-bone metaphyses, CC pear-shaped vertebral bodies, and characteristic morphology of the CC growth plate, in which the chondrocytes have a fibroblastic appearance CC and there are regions of fibrous cartilage extracellular matrix. CC Clinical features include a flat midface with a small nose and CC anteverted nares, significant shortening of all limb segments but CC relatively normal hands and feet, and a small bell-shaped thorax with a CC protuberant abdomen. {ECO:0000269|PubMed:21035103}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Deafness, autosomal dominant, 37 (DFNA37) [MIM:618533]: A form CC of non-syndromic sensorineural hearing loss. Sensorineural deafness CC results from damage to the neural receptors of the inner ear, the nerve CC pathways to the brain, or the area of the brain that receives sound CC information. DFNA37 is a slowly progressive, postlingual form. CC {ECO:0000269|PubMed:30245514}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. 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; J04177; AAA51891.1; -; mRNA. DR EMBL; AF101112; AAF04724.1; -; Genomic_DNA. DR EMBL; AF101079; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101080; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101081; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101082; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101083; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101084; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101085; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101086; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101087; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101088; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101089; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101090; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101091; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101092; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101093; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101094; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101095; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101096; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101097; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101098; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101099; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101100; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101101; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101102; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101103; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101104; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101105; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101106; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101107; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101108; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101109; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101110; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101111; AAF04724.1; JOINED; Genomic_DNA. DR EMBL; AF101112; AAF04725.1; -; Genomic_DNA. DR EMBL; AF101079; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101080; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101081; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101082; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101083; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101084; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101085; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101086; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101087; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101088; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101089; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101090; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101091; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101092; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101093; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101094; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101095; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101096; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101097; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101098; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101099; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101100; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101101; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101102; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101103; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101104; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101105; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101106; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101107; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101108; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101109; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101110; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101111; AAF04725.1; JOINED; Genomic_DNA. DR EMBL; AF101112; AAF04726.1; -; Genomic_DNA. DR EMBL; AF101079; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101080; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101081; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101082; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101083; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101084; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101085; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101086; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101087; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101088; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101089; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101090; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101091; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101092; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101093; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101094; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101095; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101096; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101097; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101098; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101099; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101100; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101101; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101102; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101103; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101104; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101105; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101106; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101107; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101108; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101109; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101110; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AF101111; AAF04726.1; JOINED; Genomic_DNA. DR EMBL; AC093150; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099567; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL627203; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72908.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72910.1; -; Genomic_DNA. DR EMBL; BC117697; AAI17698.1; -; mRNA. DR EMBL; L38956; AAA79171.1; -; Genomic_DNA. DR CCDS; CCDS53348.1; -. [P12107-3] DR CCDS; CCDS778.1; -. [P12107-1] DR CCDS; CCDS780.2; -. [P12107-4] DR PIR; A35239; CGHU1E. DR RefSeq; NP_001177638.1; NM_001190709.1. [P12107-3] DR RefSeq; NP_001845.3; NM_001854.3. [P12107-1] DR RefSeq; NP_542196.2; NM_080629.2. [P12107-2] DR RefSeq; NP_542197.3; NM_080630.3. [P12107-4] DR AlphaFoldDB; P12107; -. DR SMR; P12107; -. DR BioGRID; 107698; 19. DR ComplexPortal; CPX-1750; Collagen type XI trimer variant 1. DR ComplexPortal; CPX-1751; Collagen type XI trimer variant 2. DR ComplexPortal; CPX-1752; Collagen type XI trimer variant 3. DR IntAct; P12107; 2. DR STRING; 9606.ENSP00000359114; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1130; 1 N-Linked glycan (1 site). DR GlyCosmos; P12107; 2 sites, 2 glycans. DR GlyGen; P12107; 4 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (3 sites). DR iPTMnet; P12107; -. DR PhosphoSitePlus; P12107; -. DR BioMuta; COL11A1; -. DR DMDM; 215274245; -. DR CPTAC; CPTAC-1201; -. DR CPTAC; CPTAC-1202; -. DR jPOST; P12107; -. DR MassIVE; P12107; -. DR MaxQB; P12107; -. DR PaxDb; 9606-ENSP00000359114; -. DR PeptideAtlas; P12107; -. DR ProteomicsDB; 19514; -. DR ProteomicsDB; 52826; -. [P12107-1] DR ProteomicsDB; 52827; -. [P12107-2] DR ProteomicsDB; 52828; -. [P12107-3] DR ABCD; P12107; 1 sequenced antibody. DR Antibodypedia; 33704; 177 antibodies from 30 providers. DR DNASU; 1301; -. DR Ensembl; ENST00000353414.8; ENSP00000302551.6; ENSG00000060718.22. [P12107-3] DR Ensembl; ENST00000358392.6; ENSP00000351163.2; ENSG00000060718.22. [P12107-2] DR Ensembl; ENST00000370096.9; ENSP00000359114.3; ENSG00000060718.22. [P12107-1] DR Ensembl; ENST00000512756.5; ENSP00000426533.1; ENSG00000060718.22. [P12107-4] DR GeneID; 1301; -. DR KEGG; hsa:1301; -. DR MANE-Select; ENST00000370096.9; ENSP00000359114.3; NM_001854.4; NP_001845.3. DR UCSC; uc001dul.4; human. [P12107-1] DR AGR; HGNC:2186; -. DR CTD; 1301; -. DR DisGeNET; 1301; -. DR GeneCards; COL11A1; -. DR GeneReviews; COL11A1; -. DR HGNC; HGNC:2186; COL11A1. DR HPA; ENSG00000060718; Tissue enhanced (placenta, retina). DR MalaCards; COL11A1; -. DR MIM; 120280; gene. DR MIM; 154780; phenotype. DR MIM; 228520; phenotype. DR MIM; 604841; phenotype. DR MIM; 618533; phenotype. DR neXtProt; NX_P12107; -. DR OpenTargets; ENSG00000060718; -. DR Orphanet; 440354; Autosomal dominant myopia-midfacial retrusion-sensorineural hearing loss-rhizomelic dysplasia syndrome. DR Orphanet; 2021; Fibrochondrogenesis. DR Orphanet; 560; Marshall syndrome. DR Orphanet; 90654; Stickler syndrome type 2. DR PharmGKB; PA26702; -. DR VEuPathDB; HostDB:ENSG00000060718; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000154535; -. DR HOGENOM; CLU_001074_2_1_1; -. DR InParanoid; P12107; -. DR OMA; CDTPHKD; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P12107; -. DR TreeFam; TF323987; -. DR PathwayCommons; P12107; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; P12107; -. DR SIGNOR; P12107; -. DR BioGRID-ORCS; 1301; 13 hits in 1148 CRISPR screens. DR ChiTaRS; COL11A1; human. DR GeneWiki; Collagen,_type_XI,_alpha_1; -. DR GenomeRNAi; 1301; -. DR Pharos; P12107; Tbio. DR PRO; PR:P12107; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P12107; Protein. DR Bgee; ENSG00000060718; Expressed in tibia and 145 other cell types or tissues. DR ExpressionAtlas; P12107; baseline and differential. DR GO; GO:0005592; C:collagen type XI trimer; IDA: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:0050840; F:extracellular matrix binding; NAS:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:1904399; F:heparan sulfate binding; IEA:Ensembl. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB. DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl. DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB. DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR GO; GO:0035989; P:tendon development; IEA:Ensembl. DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IMP:UniProtKB. DR CDD; cd00110; LamG; 1. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF42; COLLAGEN ALPHA-1(XI) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 5. DR Pfam; PF02210; Laminin_G_2; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00282; LamG; 1. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR Genevisible; P12107; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cataract; Collagen; Deafness; KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism; KW Ectodermal dysplasia; Extracellular matrix; Glycoprotein; Hydroxylation; KW Metal-binding; Non-syndromic deafness; Reference proteome; Repeat; KW Secreted; Signal; Stickler syndrome. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT PROPEP 36..511 FT /note="N-terminal propeptide" FT /evidence="ECO:0000255" FT /id="PRO_0000005774" FT CHAIN 512..1563 FT /note="Collagen alpha-1(XI) chain" FT /id="PRO_0000005775" FT PROPEP 1564..1806 FT /note="C-terminal propeptide" FT /id="PRO_0000005776" FT DOMAIN 71..243 FT /note="Laminin G-like" FT DOMAIN 442..490 FT /note="Collagen-like 1" FT DOMAIN 532..586 FT /note="Collagen-like 2" FT DOMAIN 583..641 FT /note="Collagen-like 3" FT DOMAIN 616..674 FT /note="Collagen-like 4" FT DOMAIN 643..699 FT /note="Collagen-like 5" FT DOMAIN 1393..1450 FT /note="Collagen-like 6" FT DOMAIN 1429..1487 FT /note="Collagen-like 7" FT DOMAIN 1483..1541 FT /note="Collagen-like 8" FT DOMAIN 1577..1805 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 230..419 FT /note="Nonhelical region" FT REGION 420..508 FT /note="Triple-helical region (interrupted)" FT REGION 439..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 509..511 FT /note="Short nonhelical segment" FT REGION 512..528 FT /note="Telopeptide" FT REGION 527..1563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 529..1542 FT /note="Triple-helical region" FT REGION 1543..1563 FT /note="Nonhelical region (C-terminal)" FT COMPBIAS 458..484 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 680..714 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..786 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..943 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1126..1140 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1217..1231 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1291..1324 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1342..1363 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1493..1509 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1625 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1627 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1628 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1630 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1633 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 612 FT /note="Allysine" FT /evidence="ECO:0000305|PubMed:3182841" FT MOD_RES 1452 FT /note="Allysine" FT /evidence="ECO:0000305|PubMed:3182841" FT CARBOHYD 1640 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 61..243 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 182..236 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1607..1639 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1630 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1648..1803 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1714..1757 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VAR_SEQ 261..299 FT /note="YAPEDIIEYDYEYGEAEYKEAESVTEGPTVTEETIAQTE -> KKKSNFKKK FT MRTVATKSKEKSKKFTPPKSEKFSSKKKKSYQASAKAKLGVK (in isoform B)" FT /evidence="ECO:0000305" FT /id="VSP_001145" FT VAR_SEQ 261..299 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000305" FT /id="VSP_001146" FT VAR_SEQ 300..415 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046318" FT VARIANT 8 FT /note="W -> G (in dbSNP:rs12025888)" FT /id="VAR_047723" FT VARIANT 46 FT /note="D -> E (in dbSNP:rs11164663)" FT /id="VAR_047724" FT VARIANT 559 FT /note="G -> S (in dbSNP:rs12143815)" FT /id="VAR_047725" FT VARIANT 565 FT /note="G -> V (in STL2)" FT /evidence="ECO:0000269|PubMed:20513134" FT /id="VAR_063675" FT VARIANT 625 FT /note="G -> V (in STL2; dbSNP:rs121912943)" FT /evidence="ECO:0000269|PubMed:8872475" FT /id="VAR_013583" FT VARIANT 676 FT /note="G -> R (in STL2; overlapping phenotype with Marshall FT syndrome; dbSNP:rs749663226)" FT /evidence="ECO:0000269|PubMed:10486316" FT /id="VAR_013584" FT VARIANT 796 FT /note="G -> R (in FBCG1)" FT /evidence="ECO:0000269|PubMed:21035103" FT /id="VAR_065904" FT VARIANT 921..926 FT /note="Missing (in STL2; overlapping phenotype with FT Marshall syndrome)" FT /evidence="ECO:0000269|PubMed:10486316" FT /id="VAR_013585" FT VARIANT 1027 FT /note="G -> R (in STL2)" FT /evidence="ECO:0000269|PubMed:20513134" FT /id="VAR_063676" FT VARIANT 1042 FT /note="G -> R (in FBCG1)" FT /evidence="ECO:0000269|PubMed:21035103" FT /id="VAR_065905" FT VARIANT 1110..1118 FT /note="Missing (in STL2)" FT /evidence="ECO:0000269|PubMed:20513134" FT /id="VAR_063677" FT VARIANT 1313..1315 FT /note="Missing (in STL2; overlapping phenotype with FT Marshall syndrome)" FT /evidence="ECO:0000269|PubMed:10486316" FT /id="VAR_013586" FT VARIANT 1323 FT /note="P -> L (in dbSNP:rs3753841)" FT /evidence="ECO:0000269|PubMed:10486316, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1690726" FT /id="VAR_047726" FT VARIANT 1326 FT /note="A -> V (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035743" FT VARIANT 1328 FT /note="Q -> K (in a breast cancer sample; somatic mutation; FT dbSNP:rs750014974)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035744" FT VARIANT 1328 FT /note="Q -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035745" FT VARIANT 1513 FT /note="G -> D (in STL2; dbSNP:rs1553193913)" FT /evidence="ECO:0000269|PubMed:20513134" FT /id="VAR_063678" FT VARIANT 1516 FT /note="G -> V (in STL2; overlapping phenotype with Marshall FT syndrome; dbSNP:rs1553193910)" FT /evidence="ECO:0000269|PubMed:10486316, FT ECO:0000269|PubMed:20513134" FT /id="VAR_013587" FT VARIANT 1535 FT /note="S -> P (in dbSNP:rs1676486)" FT /evidence="ECO:0000269|PubMed:10486316, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1690726, FT ECO:0000269|Ref.4" FT /id="VAR_047727" FT VARIANT 1805 FT /note="L -> F (in dbSNP:rs1975916)" FT /id="VAR_047728" FT CONFLICT 941..944 FT /note="KDGL -> RMGC (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 986 FT /note="H -> Y (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 1074 FT /note="P -> R (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 1142 FT /note="D -> G (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 1218 FT /note="M -> W (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 1758 FT /note="A -> T (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" FT CONFLICT 1786 FT /note="N -> S (in Ref. 1; AAA51891)" FT /evidence="ECO:0000305" SQ SEQUENCE 1806 AA; 181065 MW; 7CBF744263321B43 CRC64; MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS PDCDSSAPKA AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS QRKNSEDTLY ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE FGPGVPAETD ITETSINGHG AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP GADGLPGPPG TMLMLPFRYG GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP GPVGGPGSSG AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP RGLLGPRGTP GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG LPGPQGPIGP PGEKGPQGKP GLAGLPGADG PPGHPGKEGQ SGEKGALGPP GPQGPIGYPG PRGVKGADGV RGLKGSKGEK GEDGFPGFKG DMGLKGDRGE VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP GLPGYPGRQG PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG AAGKEGAKGD PGPQGISGKD GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK GDKGENGPPG PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG VGEKGEPGEA GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG DDGPKGNPGP VGFPGDPGPP GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK GEAGAEGPPG KTGPVGPQGP AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP GLKGDPGSKG EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS SKKTRRHTEG MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ TNPARTCKDL QLSHPDFPDG EYWIDPNQGC SGDSFKVYCN FTSGGETCIY PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL LSYLDVEGNS INMVQMTFLK LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE EMSYDNNPFI KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG PVCFLG //