P12107 (COBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XI) chain

Gene names

Name:	COL11A1
Synonyms:	COLL6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1806 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Subunit structure	Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II).
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Cartilage, placenta and some tumor or virally transformed cell lines. Isoforms using exon IIA or IIB are found in the cartilage while isoforms using only exon IIB are found in the tendon.
Domain	The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. N-glycosylated By similarity.
Involvement in disease	Stickler syndrome 2 (STL2) [MIM:604841]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.8 Ref.11 Marshall syndrome (MRSHS) [MIM:154780]: An autosomal dominant disorder characterized by ocular abnormalities, deafness, craniofacial anomalies, and anhidrotic ectodermal dysplasia. Clinical features include short stature; flat or retruded midface with short, depressed nose, flat nasal bridge and anteverted nares; cleft palate with or without the Pierre Robin sequence; appearance of large eyes with ocular hypertelorism; cataracts, either congenital or juvenile; esotropia; high myopia; sensorineural hearing loss; spondyloepiphyseal abnormalities; calcification of the falx cerebri; ectodermal abnormalities, including defects in sweating and dental structures. Note: The disease is caused by mutations affecting the gene represented in this entry. Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10
Sequence similarities	Belongs to the fibrillar collagen family. Contains 8 collagen-like domains. Contains 1 fibrillar collagen NC1 domain. Contains 1 laminin G-like domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cataract Deafness Disease mutation Dwarfism Ectodermal dysplasia Stickler syndrome
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cartilage condensation Inferred from electronic annotation. Source: Compara chondrocyte development Inferred from electronic annotation. Source: Compara collagen fibril organization Non-traceable author statement Ref.6. Source: UniProtKB detection of mechanical stimulus involved in sensory perception of sound Inferred from mutant phenotype PubMed 10889003. Source: UniProtKB embryonic skeletal system morphogenesis Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from electronic annotation. Source: Compara proteoglycan metabolic process Inferred from electronic annotation. Source: Compara ventricular cardiac muscle tissue morphogenesis Inferred from electronic annotation. Source: Compara visual perception Inferred from mutant phenotype PubMed 10573014Ref.8. Source: UniProtKB
Cellular_component	collagen type XI Inferred from direct assay Ref.6. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix binding Non-traceable author statement Ref.6. Source: UniProtKB extracellular matrix structural constituent Non-traceable author statement Ref.2. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding, bridging Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. There is alternative usage of exon IIA or exon IIB. Transcripts containing exon IIA or IIB are present in cartilage, but exon IIB is preferentially utilized in transcripts from tendon.

Isoform A (identifier: P12107-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P12107-2)

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: YAPEDIIEYD...VTEETIAQTE → KKKSNFKKKM...ASAKAKLGVK

Isoform C (identifier: P12107-3)

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: Missing.

Isoform 4 (identifier: P12107-4)

The sequence of this isoform differs from the canonical sequence as follows:
     300-415: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Propeptide	36 – 511	476	N-terminal propeptide Potential		PRO_0000005774
	Chain	512 – 1563	1052	Collagen alpha-1(XI) chain		PRO_0000005775
	Propeptide	1564 – 1806	243	C-terminal propeptide		PRO_0000005776
Regions
	Domain	71 – 243	173	Laminin G-like
	Domain	442 – 490	49	Collagen-like 1
	Domain	532 – 586	55	Collagen-like 2
	Domain	583 – 641	59	Collagen-like 3
	Domain	616 – 674	59	Collagen-like 4
	Domain	643 – 699	57	Collagen-like 5
	Domain	1393 – 1450	58	Collagen-like 6
	Domain	1429 – 1487	59	Collagen-like 7
	Domain	1483 – 1541	59	Collagen-like 8
	Domain	1577 – 1805	229	Fibrillar collagen NC1
	Region	230 – 419	190	Nonhelical region
	Region	420 – 508	89	Triple-helical region (interrupted)
	Region	509 – 511	3	Short nonhelical segment
	Region	512 – 528	17	Telopeptide
	Region	529 – 1542	1014	Triple-helical region
	Region	1543 – 1563	21	Nonhelical region (C-terminal)
Sites
	Metal binding	1625	1	Calcium By similarity
	Metal binding	1627	1	Calcium By similarity
	Metal binding	1628	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1630	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1633	1	Calcium By similarity
Amino acid modifications
	Modified residue	612	1	Allysine
	Modified residue	1452	1	Allysine
	Glycosylation	1640	1	N-linked (GlcNAc...) Potential
	Disulfide bond	61 ↔ 243		By similarity
	Disulfide bond	182 ↔ 236		By similarity
	Disulfide bond	1607 ↔ 1639		By similarity
	Disulfide bond	1630		Interchain By similarity
	Disulfide bond	1648 ↔ 1803		By similarity
	Disulfide bond	1714 ↔ 1757		By similarity
Natural variations
	Alternative sequence	261 – 299	39	YAPED…IAQTE → KKKSNFKKKMRTVATKSKEK SKKFTPPKSEKFSSKKKKSY QASAKAKLGVK in isoform B.		VSP_001145
	Alternative sequence	261 – 299	39	Missing in isoform C.		VSP_001146
	Alternative sequence	300 – 415	116	Missing in isoform 4.		VSP_046318
	Natural variant	8	1	W → G. Corresponds to variant rs12025888 [ dbSNP | Ensembl ].		VAR_047723
	Natural variant	46	1	D → E. Corresponds to variant rs11164663 [ dbSNP | Ensembl ].		VAR_047724
	Natural variant	559	1	G → S. Corresponds to variant rs12143815 [ dbSNP | Ensembl ].		VAR_047725
	Natural variant	565	1	G → V in STL2. Ref.11		VAR_063675
	Natural variant	625	1	G → V in STL2. Ref.8		VAR_013583
	Natural variant	676	1	G → R in STL2; overlapping phenotype with Marshall syndrome. Ref.2		VAR_013584
	Natural variant	796	1	G → R in FBCG1. Ref.10		VAR_065904
	Natural variant	921 – 926	6	Missing in STL2; overlapping phenotype with Marshall syndrome.		VAR_013585
	Natural variant	1027	1	G → R in STL2. Ref.11		VAR_063676
	Natural variant	1042	1	G → R in FBCG1. Ref.10		VAR_065905
	Natural variant	1110 – 1118	9	Missing in STL2.		VAR_063677
	Natural variant	1313 – 1315	3	Missing in STL2; overlapping phenotype with Marshall syndrome.		VAR_013586
	Natural variant	1323	1	P → L. Ref.1 Ref.2 Ref.5 Corresponds to variant rs3753841 [ dbSNP | Ensembl ].		VAR_047726
	Natural variant	1326	1	A → V in a breast cancer sample; somatic mutation. Ref.9		VAR_035743
	Natural variant	1328	1	Q → K in a breast cancer sample; somatic mutation. Ref.9		VAR_035744
	Natural variant	1328	1	Q → L in a breast cancer sample; somatic mutation. Ref.9		VAR_035745
	Natural variant	1513	1	G → D in STL2. Ref.11		VAR_063678
	Natural variant	1516	1	G → V in STL2; overlapping phenotype with Marshall syndrome. Ref.2 Ref.11		VAR_013587
	Natural variant	1535	1	S → P. Ref.1 Ref.2 Ref.4 Ref.5 Corresponds to variant rs1676486 [ dbSNP | Ensembl ].		VAR_047727
	Natural variant	1805	1	L → F. Corresponds to variant rs1975916 [ dbSNP | Ensembl ].		VAR_047728
Experimental info
	Sequence conflict	941 – 944	4	KDGL → RMGC in AAA51891. Ref.1
	Sequence conflict	986	1	H → Y in AAA51891. Ref.1
	Sequence conflict	1074	1	P → R in AAA51891. Ref.1
	Sequence conflict	1142	1	D → G in AAA51891. Ref.1
	Sequence conflict	1218	1	M → W in AAA51891. Ref.1
	Sequence conflict	1758	1	A → T in AAA51891. Ref.1
	Sequence conflict	1786	1	N → S in AAA51891. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 7CBF744263321B43	FASTA	1,806	181,065
	10 20 30 40 50 60 MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF 70 80 90 100 110 120 CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN 130 140 150 160 170 180 EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV 190 200 210 220 230 240 DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS 250 260 270 280 290 300 PDCDSSAPKA AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA 310 320 330 340 350 360 NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS QRKNSEDTLY 370 380 390 400 410 420 ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE FGPGVPAETD ITETSINGHG 430 440 450 460 470 480 AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP 490 500 510 520 530 540 GADGLPGPPG TMLMLPFRYG GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP 550 560 570 580 590 600 GPVGGPGSSG AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR 610 620 630 640 650 660 GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP RGLLGPRGTP 670 680 690 700 710 720 GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG LPGPQGPIGP PGEKGPQGKP 730 740 750 760 770 780 GLAGLPGADG PPGHPGKEGQ SGEKGALGPP GPQGPIGYPG PRGVKGADGV RGLKGSKGEK 790 800 810 820 830 840 GEDGFPGFKG DMGLKGDRGE VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP 850 860 870 880 890 900 GLPGYPGRQG PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP 910 920 930 940 950 960 GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT 970 980 990 1000 1010 1020 GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG AAGKEGAKGD PGPQGISGKD 1030 1040 1050 1060 1070 1080 GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ 1090 1100 1110 1120 1130 1140 GPPGPAGEKG APGEKGPQGP AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK 1150 1160 1170 1180 1190 1200 GDKGENGPPG PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ 1210 1220 1230 1240 1250 1260 GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG VGEKGEPGEA 1270 1280 1290 1300 1310 1320 GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG DDGPKGNPGP VGFPGDPGPP 1330 1340 1350 1360 1370 1380 GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK 1390 1400 1410 1420 1430 1440 GEAGAEGPPG KTGPVGPQGP AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP 1450 1460 1470 1480 1490 1500 GLKGDPGSKG EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP 1510 1520 1530 1540 1550 1560 GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS SKKTRRHTEG 1570 1580 1590 1600 1610 1620 MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ TNPARTCKDL QLSHPDFPDG 1630 1640 1650 1660 1670 1680 EYWIDPNQGC SGDSFKVYCN FTSGGETCIY PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL 1690 1700 1710 1720 1730 1740 LSYLDVEGNS INMVQMTFLK LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE 1750 1760 1770 1780 1790 1800 EMSYDNNPFI KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG PVCFLG
	Isoform B [UniParc]. Checksum: D86BD1303BA45C99	FASTA	1,818	182,422
	10 20 30 40 50 60 MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF 70 80 90 100 110 120 CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN 130 140 150 160 170 180 EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV 190 200 210 220 230 240 DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS 250 260 270 280 290 300 PDCDSSAPKA AQAQEPQIDE KKKSNFKKKM RTVATKSKEK SKKFTPPKSE KFSSKKKKSY 310 320 330 340 350 360 QASAKAKLGV KANIVDDFQE YNYGTMESYQ TEAPRHVSGT NEPNPVEEIF TEEYLTGEDY 370 380 390 400 410 420 DSQRKNSEDT LYENKEIDGR DSDLLVDGDL GEYDFYEYKE YEDKPTSPPN EEFGPGVPAE 430 440 450 460 470 480 TDITETSING HGAYGEKGQK GEPAVVEPGM LVEGPPGPAG PAGIMGPPGL QGPTGPPGDP 490 500 510 520 530 540 GDRGPPGRPG LPGADGLPGP PGTMLMLPFR YGGDGSKGPT ISAQEAQAQA ILQQARIALR 550 560 570 580 590 600 GPPGPMGLTG RPGPVGGPGS SGAKGESGDP GPQGPRGVQG PPGPTGKPGK RGRPGADGGR 610 620 630 640 650 660 GMPGEPGAKG DRGFDGLPGL PGDKGHRGER GPQGPPGPPG DDGMRGEDGE IGPRGLPGEA 670 680 690 700 710 720 GPRGLLGPRG TPGAPGQPGM AGVDGPPGPK GNMGPQGEPG PPGQQGNPGP QGLPGPQGPI 730 740 750 760 770 780 GPPGEKGPQG KPGLAGLPGA DGPPGHPGKE GQSGEKGALG PPGPQGPIGY PGPRGVKGAD 790 800 810 820 830 840 GVRGLKGSKG EKGEDGFPGF KGDMGLKGDR GEVGQIGPRG EDGPEGPKGR AGPTGDPGPS 850 860 870 880 890 900 GQAGEKGKLG VPGLPGYPGR QGPKGSTGFP GFPGANGEKG ARGVAGKPGP RGQRGPTGPR 910 920 930 940 950 960 GSRGARGPTG KPGPKGTSGG DGPPGPPGER GPQGPQGPVG FPGPKGPPGP PGKDGLPGHP 970 980 990 1000 1010 1020 GQRGETGFQG KTGPPGPGGV VGPQGPTGET GPIGERGHPG PPGPPGEQGL PGAAGKEGAK 1030 1040 1050 1060 1070 1080 GDPGPQGISG KDGPAGLRGF PGERGLPGAQ GAPGLKGGEG PQGPPGPVGS PGERGSAGTA 1090 1100 1110 1120 1130 1140 GPIGLPGRPG PQGPPGPAGE KGAPGEKGPQ GPAGRDGVQG PVGLPGPAGP AGSPGEDGDK 1150 1160 1170 1180 1190 1200 GEIGEPGQKG SKGDKGENGP PGPPGLQGPV GAPGIAGGDG EPGPRGQQGM FGQKGDEGAR 1210 1220 1230 1240 1250 1260 GFPGPPGPIG LQGLPGPPGE KGENGDVGPM GPPGPPGPRG PQGPNGADGP QGPPGSVGSV 1270 1280 1290 1300 1310 1320 GGVGEKGEPG EAGNPGPPGE AGVGGPKGER GEKGEAGPPG AAGPPGAKGP PGDDGPKGNP 1330 1340 1350 1360 1370 1380 GPVGFPGDPG PPGEPGPAGQ DGVGGDKGED GDPGQPGPPG PSGEAGPPGP PGKRGPPGAA 1390 1400 1410 1420 1430 1440 GAEGRQGEKG AKGEAGAEGP PGKTGPVGPQ GPAGKPGPEG LRGIPGPVGE QGLPGAAGQD 1450 1460 1470 1480 1490 1500 GPPGPMGPPG LPGLKGDPGS KGEKGHPGLI GLIGPPGEQG EKGDRGLPGT QGSPGAKGDG 1510 1520 1530 1540 1550 1560 GIPGPAGPLG PPGPPGLPGP QGPKGNKGST GPAGQKGDSG LPGPPGSPGP PGEVIQPLPI 1570 1580 1590 1600 1610 1620 LSSKKTRRHT EGMQADADDN ILDYSDGMEE IFGSLNSLKQ DIEHMKFPMG TQTNPARTCK 1630 1640 1650 1660 1670 1680 DLQLSHPDFP DGEYWIDPNQ GCSGDSFKVY CNFTSGGETC IYPDKKSEGV RISSWPKEKP 1690 1700 1710 1720 1730 1740 GSWFSEFKRG KLLSYLDVEG NSINMVQMTF LKLLTASARQ NFTYHCHQSA AWYDVSSGSY 1750 1760 1770 1780 1790 1800 DKALRFLGSN DEEMSYDNNP FIKTLYDGCA SRKGYEKTVI EINTPKIDQV PIVDVMINDF 1810 GDQNQKFGFE VGPVCFLG
	Isoform C [UniParc]. Checksum: DE451EE638FDBCA9	FASTA	1,767	176,619
	10 20 30 40 50 60 MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF 70 80 90 100 110 120 CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN 130 140 150 160 170 180 EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV 190 200 210 220 230 240 DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS 250 260 270 280 290 300 PDCDSSAPKA AQAQEPQIDE ANIVDDFQEY NYGTMESYQT EAPRHVSGTN EPNPVEEIFT 310 320 330 340 350 360 EEYLTGEDYD SQRKNSEDTL YENKEIDGRD SDLLVDGDLG EYDFYEYKEY EDKPTSPPNE 370 380 390 400 410 420 EFGPGVPAET DITETSINGH GAYGEKGQKG EPAVVEPGML VEGPPGPAGP AGIMGPPGLQ 430 440 450 460 470 480 GPTGPPGDPG DRGPPGRPGL PGADGLPGPP GTMLMLPFRY GGDGSKGPTI SAQEAQAQAI 490 500 510 520 530 540 LQQARIALRG PPGPMGLTGR PGPVGGPGSS GAKGESGDPG PQGPRGVQGP PGPTGKPGKR 550 560 570 580 590 600 GRPGADGGRG MPGEPGAKGD RGFDGLPGLP GDKGHRGERG PQGPPGPPGD DGMRGEDGEI 610 620 630 640 650 660 GPRGLPGEAG PRGLLGPRGT PGAPGQPGMA GVDGPPGPKG NMGPQGEPGP PGQQGNPGPQ 670 680 690 700 710 720 GLPGPQGPIG PPGEKGPQGK PGLAGLPGAD GPPGHPGKEG QSGEKGALGP PGPQGPIGYP 730 740 750 760 770 780 GPRGVKGADG VRGLKGSKGE KGEDGFPGFK GDMGLKGDRG EVGQIGPRGE DGPEGPKGRA 790 800 810 820 830 840 GPTGDPGPSG QAGEKGKLGV PGLPGYPGRQ GPKGSTGFPG FPGANGEKGA RGVAGKPGPR 850 860 870 880 890 900 GQRGPTGPRG SRGARGPTGK PGPKGTSGGD GPPGPPGERG PQGPQGPVGF PGPKGPPGPP 910 920 930 940 950 960 GKDGLPGHPG QRGETGFQGK TGPPGPGGVV GPQGPTGETG PIGERGHPGP PGPPGEQGLP 970 980 990 1000 1010 1020 GAAGKEGAKG DPGPQGISGK DGPAGLRGFP GERGLPGAQG APGLKGGEGP QGPPGPVGSP 1030 1040 1050 1060 1070 1080 GERGSAGTAG PIGLPGRPGP QGPPGPAGEK GAPGEKGPQG PAGRDGVQGP VGLPGPAGPA 1090 1100 1110 1120 1130 1140 GSPGEDGDKG EIGEPGQKGS KGDKGENGPP GPPGLQGPVG APGIAGGDGE PGPRGQQGMF 1150 1160 1170 1180 1190 1200 GQKGDEGARG FPGPPGPIGL QGLPGPPGEK GENGDVGPMG PPGPPGPRGP QGPNGADGPQ 1210 1220 1230 1240 1250 1260 GPPGSVGSVG GVGEKGEPGE AGNPGPPGEA GVGGPKGERG EKGEAGPPGA AGPPGAKGPP 1270 1280 1290 1300 1310 1320 GDDGPKGNPG PVGFPGDPGP PGEPGPAGQD GVGGDKGEDG DPGQPGPPGP SGEAGPPGPP 1330 1340 1350 1360 1370 1380 GKRGPPGAAG AEGRQGEKGA KGEAGAEGPP GKTGPVGPQG PAGKPGPEGL RGIPGPVGEQ 1390 1400 1410 1420 1430 1440 GLPGAAGQDG PPGPMGPPGL PGLKGDPGSK GEKGHPGLIG LIGPPGEQGE KGDRGLPGTQ 1450 1460 1470 1480 1490 1500 GSPGAKGDGG IPGPAGPLGP PGPPGLPGPQ GPKGNKGSTG PAGQKGDSGL PGPPGSPGPP 1510 1520 1530 1540 1550 1560 GEVIQPLPIL SSKKTRRHTE GMQADADDNI LDYSDGMEEI FGSLNSLKQD IEHMKFPMGT 1570 1580 1590 1600 1610 1620 QTNPARTCKD LQLSHPDFPD GEYWIDPNQG CSGDSFKVYC NFTSGGETCI YPDKKSEGVR 1630 1640 1650 1660 1670 1680 ISSWPKEKPG SWFSEFKRGK LLSYLDVEGN SINMVQMTFL KLLTASARQN FTYHCHQSAA 1690 1700 1710 1720 1730 1740 WYDVSSGSYD KALRFLGSND EEMSYDNNPF IKTLYDGCAS RKGYEKTVIE INTPKIDQVP 1750 1760 IVDVMINDFG DQNQKFGFEV GPVCFLG
	Isoform 4 [UniParc]. Checksum: A612FE4054F2F34E	FASTA	1,690	167,752
	10 20 30 40 50 60 MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF 70 80 90 100 110 120 CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN 130 140 150 160 170 180 EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV 190 200 210 220 230 240 DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS 250 260 270 280 290 300 PDCDSSAPKA AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEI 310 320 330 340 350 360 NGHGAYGEKG QKGEPAVVEP GMLVEGPPGP AGPAGIMGPP GLQGPTGPPG DPGDRGPPGR 370 380 390 400 410 420 PGLPGADGLP GPPGTMLMLP FRYGGDGSKG PTISAQEAQA QAILQQARIA LRGPPGPMGL 430 440 450 460 470 480 TGRPGPVGGP GSSGAKGESG DPGPQGPRGV QGPPGPTGKP GKRGRPGADG GRGMPGEPGA 490 500 510 520 530 540 KGDRGFDGLP GLPGDKGHRG ERGPQGPPGP PGDDGMRGED GEIGPRGLPG EAGPRGLLGP 550 560 570 580 590 600 RGTPGAPGQP GMAGVDGPPG PKGNMGPQGE PGPPGQQGNP GPQGLPGPQG PIGPPGEKGP 610 620 630 640 650 660 QGKPGLAGLP GADGPPGHPG KEGQSGEKGA LGPPGPQGPI GYPGPRGVKG ADGVRGLKGS 670 680 690 700 710 720 KGEKGEDGFP GFKGDMGLKG DRGEVGQIGP RGEDGPEGPK GRAGPTGDPG PSGQAGEKGK 730 740 750 760 770 780 LGVPGLPGYP GRQGPKGSTG FPGFPGANGE KGARGVAGKP GPRGQRGPTG PRGSRGARGP 790 800 810 820 830 840 TGKPGPKGTS GGDGPPGPPG ERGPQGPQGP VGFPGPKGPP GPPGKDGLPG HPGQRGETGF 850 860 870 880 890 900 QGKTGPPGPG GVVGPQGPTG ETGPIGERGH PGPPGPPGEQ GLPGAAGKEG AKGDPGPQGI 910 920 930 940 950 960 SGKDGPAGLR GFPGERGLPG AQGAPGLKGG EGPQGPPGPV GSPGERGSAG TAGPIGLPGR 970 980 990 1000 1010 1020 PGPQGPPGPA GEKGAPGEKG PQGPAGRDGV QGPVGLPGPA GPAGSPGEDG DKGEIGEPGQ 1030 1040 1050 1060 1070 1080 KGSKGDKGEN GPPGPPGLQG PVGAPGIAGG DGEPGPRGQQ GMFGQKGDEG ARGFPGPPGP 1090 1100 1110 1120 1130 1140 IGLQGLPGPP GEKGENGDVG PMGPPGPPGP RGPQGPNGAD GPQGPPGSVG SVGGVGEKGE 1150 1160 1170 1180 1190 1200 PGEAGNPGPP GEAGVGGPKG ERGEKGEAGP PGAAGPPGAK GPPGDDGPKG NPGPVGFPGD 1210 1220 1230 1240 1250 1260 PGPPGEPGPA GQDGVGGDKG EDGDPGQPGP PGPSGEAGPP GPPGKRGPPG AAGAEGRQGE 1270 1280 1290 1300 1310 1320 KGAKGEAGAE GPPGKTGPVG PQGPAGKPGP EGLRGIPGPV GEQGLPGAAG QDGPPGPMGP 1330 1340 1350 1360 1370 1380 PGLPGLKGDP GSKGEKGHPG LIGLIGPPGE QGEKGDRGLP GTQGSPGAKG DGGIPGPAGP 1390 1400 1410 1420 1430 1440 LGPPGPPGLP GPQGPKGNKG STGPAGQKGD SGLPGPPGSP GPPGEVIQPL PILSSKKTRR 1450 1460 1470 1480 1490 1500 HTEGMQADAD DNILDYSDGM EEIFGSLNSL KQDIEHMKFP MGTQTNPART CKDLQLSHPD 1510 1520 1530 1540 1550 1560 FPDGEYWIDP NQGCSGDSFK VYCNFTSGGE TCIYPDKKSE GVRISSWPKE KPGSWFSEFK 1570 1580 1590 1600 1610 1620 RGKLLSYLDV EGNSINMVQM TFLKLLTASA RQNFTYHCHQ SAAWYDVSSG SYDKALRFLG 1630 1640 1650 1660 1670 1680 SNDEEMSYDN NPFIKTLYDG CASRKGYEKT VIEINTPKID QVPIVDVMIN DFGDQNQKFG 1690 FEVGPVCFLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and expression of the gene in tumor cell lines." Yoshioka H., Ramirez F. J. Biol. Chem. 265:6423-6426(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANTS LEU-1323 AND PRO-1535.
[2]	"Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes." Annunen S., Koerkkoe J., Czarny M., Warman M.L., Brunner H.G., Kaeaeriaeinen H., Mulliken J.B., Tranebjaerg L., Brooks D.G., Cox G.F., Cruysberg J.R., Curtis M.A., Davenport S.L.H., Friedrich C.A., Kaitila I., Krawczynski M.R., Latos-Bielenska A., Mukai S. , Olsen B.R., Shinno N., Somer M., Vikkula M., Zlotogora J., Prockop D.J., Ala-Kokko L. Am. J. Hum. Genet. 65:974-983(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B AND C), VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926 DEL; 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-1535.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS LEU-1323 AND PRO-1535.
[6]	"Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene is not restricted to cartilagenous tissue." Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T., Ninomiya Y., Olsen B.R., Ramirez F. J. Biol. Chem. 263:17159-17166(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 538-1806, PARTIAL PROTEIN SEQUENCE.
[7]	"Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains." Zhidkova N.I., Justice S.K., Mayne R. J. Biol. Chem. 270:9486-9493(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING. Tissue: Blood.
[8]	"A family with Stickler syndrome type 2 has a mutation in the COL11A1 gene resulting in the substitution of glycine 97 by valine in alpha-1(XI) collagen." Richards A.J., Yates J.R.W., Williams R., Payne S.J., Pope F.M., Scott J.D., Snead M.P. Hum. Mol. Genet. 5:1339-1343(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL2 VAL-625.
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-1326; LYS-1328 AND LEU-1328.
[10]	"Fibrochondrogenesis results from mutations in the COL11A1 type XI collagen gene." Tompson S.W., Bacino C.A., Safina N.P., Bober M.B., Proud V.K., Funari T., Wangler M.F., Nevarez L., Ala-Kokko L., Wilcox W.R., Eyre D.R., Krakow D., Cohn D.H. Am. J. Hum. Genet. 87:708-712(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FBCG1 ARG-796 AND ARG-1042.
[11]	"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1." Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S., Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P. Hum. Mutat. 31:E1461-E1471(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND VAL-1516.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04177 mRNA. Translation: AAA51891.1. AF101112 , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04724.1. AF101112 , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04725.1. AF101112 , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04726.1. AL627203, AC093150, AC099567 Genomic DNA. Translation: CAH73908.1. CH471097 Genomic DNA. Translation: EAW72908.1. CH471097 Genomic DNA. Translation: EAW72910.1. BC117697 mRNA. Translation: AAI17698.1. L38956 Genomic DNA. Translation: AAA79171.1.
IPI	IPI00218539. IPI00218540. IPI00295575. IPI00965543.
PIR	CGHU1E. A35239.
RefSeq	NP_001177638.1. NM_001190709.1. NP_001845.3. NM_001854.3. NP_542196.2. NM_080629.2. NP_542197.3. NM_080630.3.
UniGene	Hs.523446.
3D structure databases
ProteinModelPortal	P12107.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000351163.
PTM databases
PhosphoSite	P12107.
Polymorphism databases
DMDM	215274245.
Proteomic databases
PaxDb	P12107.
PRIDE	P12107.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000353414; ENSP00000302551; ENSG00000060718. ENST00000358392; ENSP00000351163; ENSG00000060718. ENST00000370096; ENSP00000359114; ENSG00000060718. ENST00000512756; ENSP00000426533; ENSG00000060718.
GeneID	1301.
KEGG	hsa:1301.
UCSC	uc001dul.3. human. uc001dum.3. human. uc001dun.3. human.
Organism-specific databases
CTD	1301.
GeneCards	GC01M103342.
H-InvDB	HIX0028847.
HGNC	HGNC:2186. COL11A1.
MIM	120280. gene. 154780. phenotype. 228520. phenotype. 604841. phenotype.
neXtProt	NX_P12107.
Orphanet	2021. Fibrochondrogenesis. 560. Marshall syndrome. 90654. Stickler syndrome type 2.
PharmGKB	PA26702.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG004933.
KO	K06236.
OMA	HPGKEGQ.
OrthoDB	EOG49GKHM.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P12107.
Bgee	P12107.
CleanEx	HS_COL11A1.
Genevestigator	P12107.
GermOnline	ENSG00000060718. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000885. Fib_collagen_C. IPR001791. Laminin_G. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 8 hits. PF02210. Laminin_G_2. 1 hit. [Graphical view]
ProDom	PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00038. COLFI. 1 hit. SM00282. LamG. 1 hit. SM00210. TSPN. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50025. LAM_G_DOMAIN. False negative. PS51461. NC1_FIB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1301.
NextBio	5283.
PMAP-CutDB	B1ASK7.
SOURCE	Search...

Entry information

Entry name

COBA1_HUMAN

Accession

Primary (citable) accession number: P12107
Secondary accession number(s): B1ASK7 , D3DT73, E9PCU0, Q14034, Q149N0, Q9UIT4, Q9UIT5, Q9UIT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 153 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.