COBA1_HUMAN
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 03-AUG-2022, entry version 229.
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}.
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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; 15.
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 GlyGen; P12107; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
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; P12107; -.
DR PeptideAtlas; P12107; -.
DR PRIDE; 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; 148 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 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; 250984; Autosomal recessive Stickler 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; 933605at2759; -.
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; 11 hits in 1065 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 143 other tissues.
DR ExpressionAtlas; P12107; baseline and differential.
DR Genevisible; P12107; HS.
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: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:0050840; F:extracellular matrix binding; NAS:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:1904399; F:heparan sulfate binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
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 InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 7.
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; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
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
