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Protein

Collagen alpha-1(XI) chain

Gene

Col11a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1623 – 16231CalciumBy similarity
Metal bindingi1625 – 16251CalciumBy similarity
Metal bindingi1626 – 16261Calcium; via carbonyl oxygenBy similarity
Metal bindingi1628 – 16281Calcium; via carbonyl oxygenBy similarity
Metal bindingi1631 – 16311CalciumBy similarity

GO - Molecular functioni

  • extracellular matrix structural constituent Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1650814. Collagen biosynthesis and modifying enzymes.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XI) chain
Gene namesi
Name:Col11a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2372. Col11a1.

Subcellular locationi

GO - Cellular componenti

  • collagen type XI trimer Source: Ensembl
  • extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence analysisAdd
BLAST
Propeptidei35 – 511477N-terminal propeptideSequence analysisPRO_0000415946Add
BLAST
Chaini512 – 15611050Collagen alpha-1(XI) chainPRO_0000005780Add
BLAST
Propeptidei1562 – 1804243C-terminal propeptidePRO_0000005781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 242PROSITE-ProRule annotation1 Publication
Disulfide bondi181 ↔ 235PROSITE-ProRule annotation1 Publication
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence analysis
Modified residuei610 – 6101AllysineBy similarity
Modified residuei1450 – 14501AllysineBy similarity
Disulfide bondi1605 ↔ 1637PROSITE-ProRule annotation
Disulfide bondi1628 – 1628InterchainPROSITE-ProRule annotation
Glycosylationi1638 – 16381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1646 ↔ 1801PROSITE-ProRule annotation
Glycosylationi1707 – 17071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1712 ↔ 1755PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP20909.
PRIDEiP20909.

PTM databases

PhosphoSiteiP20909.

Expressioni

Gene expression databases

GenevisibleiP20909. RN.

Interactioni

Subunit structurei

Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is probably a post-translational modification of alpha 1(II).

Protein-protein interaction databases

IntActiP20909. 33 interactions.
STRINGi10116.ENSRNOP00000023794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 242173Laminin G-likeAdd
BLAST
Domaini440 – 48849Collagen-like 1Add
BLAST
Domaini530 – 58455Collagen-like 2Add
BLAST
Domaini581 – 63959Collagen-like 3Add
BLAST
Domaini607 – 66458Collagen-like 4Add
BLAST
Domaini641 – 69858Collagen-like 5Add
BLAST
Domaini746 – 80459Collagen-like 6Add
BLAST
Domaini1391 – 144959Collagen-like 7Add
BLAST
Domaini1442 – 149251Collagen-like 8Add
BLAST
Domaini1481 – 153959Collagen-like 9Add
BLAST
Domaini1575 – 1803229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 417189Nonhelical regionAdd
BLAST
Regioni418 – 50689Triple-helical region (interrupted)Add
BLAST
Regioni507 – 5093Short nonhelical segment
Regioni510 – 52718TelopeptideAdd
BLAST
Regioni528 – 15401013Triple-helical regionAdd
BLAST
Regioni1541 – 156121Nonhelical region (C-terminal)Add
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 9 collagen-like domains.Curated
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG103137.
InParanoidiP20909.
KOiK19721.
OMAiHPGKEGQ.
OrthoDBiEOG7XPZ4W.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20909-1) [UniParc]FASTAAdd to basket

Also known as: +V1a+V2, p6A+8

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.

« Hide

        10         20         30         40         50
MEPWSRWKTK RWIWDLTIST LVLTFLFQAR EVRGAAPVDI LKALDFHNSP
60 70 80 90 100
VGISKTTGFC TSRKNSKDPD IAYRVTEEAQ ISAPTKQLFP GGIFPQDFSI
110 120 130 140 150
LFTIKPKKGT QAFLLSLYNE HGIQQLGVEV GRSPVFLFED HTGKPTPENY
160 170 180 190 200
PLFSTVNIAD GKWHRVAISV EKKTVTMIVD CKKKITKPLD RSERSIVDTN
210 220 230 240 250
GIMVFGTRIL ETDVFQGDIQ QFLITGDPKA AYDYCDHYSP DCDLTSKAAQ
260 270 280 290 300
AQEPHIDEYA PEDIIEYDYE YGETDYKEAE SVTEMPTVTE ETVAQTEANI
310 320 330 340 350
VDDFQDYNYG TMETYQTESP RRVSGSNEPN PVEEGFTEEY LTGEDYDVQR
360 370 380 390 400
NISEDILYGN KGIDGRDSDL LVDGDLGEYD FYEYKEYEER TTTSPNEEFG
410 420 430 440 450
PGVPAETDFT ETSINGHGAY GEKGQKGEPA VVEPGMLVEG PPGPAGPAGL
460 470 480 490 500
MGPPGLQGPS GLPGDPGDRG PPGRPGLPGA DGLPGPPGTM LMLPFRYGGD
510 520 530 540 550
GSKGPTISAQ EAQAQAILQQ ARIALRGPPG PMGLTGRPGP VGGPGSAGAK
560 570 580 590 600
GESGDPGPQG PRGVQGPPGP TGKPGKRGRP GADGGRGMPG EPGSKGDRGF
610 620 630 640 650
DGLPGLPGDK GHRGERGPQG PPGLPGDDGM RGEDGEIGPR GLPGEAGPRG
660 670 680 690 700
LLGPRGTPGP PGQPGIGGID GPQGPKGNMG PQGEPGPPGQ QGNPGPQGLP
710 720 730 740 750
GPQGPIGPPG EKGPQGKPGL AGLPGADGPP GHPGKEGQSG EKGALGPPGP
760 770 780 790 800
QGPIGYPGPR GVKGADGVRG LKGSKGEKGE DGFPGFKGDM GLKGDRGEVG
810 820 830 840 850
QVGPRGEDGP EGPKGRAGPT GDPGPSGQAG EKGKLGVPGL PGYPGRQGPK
860 870 880 890 900
GSTGFPGFPG ANGEKGARGI AGKPGPRGQR GPTGPRGSRG ARGPTGKPGP
910 920 930 940 950
KGTSGGDGPP GPPGERGPQG PQGPVGFPGP KGPPGPAGKD GLPGHPGQRG
960 970 980 990 1000
ETGFQGKTGP PGPGGVVGPQ GPTGETGPIG ERGHPGTPGP PGEQGLPGAA
1010 1020 1030 1040 1050
GKEGAKGDPG PQGISGKDGP AGIRGFPGER GLPGAQGAPG LKGGEGPQGP
1060 1070 1080 1090 1100
QGPIGSPGER GSAGTAGPIG LPGRPGPQGP PGPAGEKGAP GEKGPQGPAG
1110 1120 1130 1140 1150
RDGVQGPVGL PGPAGPAGSP GEDGDKGEIG EPGQKGSKGD KGENGPPGPP
1160 1170 1180 1190 1200
GLQGPVGAPG IAGGDGEAGP RGQQGMFGQK GDEGARGFPG PPGPIGLQGL
1210 1220 1230 1240 1250
PGPPGEKGEN GDVGPMGPPG PPGPRGPQGP NGADGPQGPP GSIGSVGGVG
1260 1270 1280 1290 1300
EKGEPGEAGN PGPPGEAGSG GPKGERGEKG EAGPPGAAGP PGIKGPPGDD
1310 1320 1330 1340 1350
GPKGNPGPVG FPGDPGPPGE PGPAGQDGVG GDKGEDGDPG QPGPPGPSGE
1360 1370 1380 1390 1400
AGPPGPPGKR GPPGASGSEG RQGEKGAKGE AGAEGPPGKT GPVGPQGPSG
1410 1420 1430 1440 1450
KPGPEGLRGI PGPVGEQGLP GAAGQDGPPG PLGPPGLPGL KGDPGSKGEK
1460 1470 1480 1490 1500
GHPGLIGLIG PPGEQGEKGD RGLPGTQGSP GAKGDGGIPG PAGPIGPPGP
1510 1520 1530 1540 1550
PGLPGPAGPK GNKGSSGPTG QKGDSGMPGP PGPPGPPGEV IQPLPILSPK
1560 1570 1580 1590 1600
KTRRHTESIQ ADAGDNILDY SDGMEEIFGS LNSLKQDIEH MKFPMGTQTN
1610 1620 1630 1640 1650
PARTCKDLQL SHPDFPDGEY WIDPNQGCSG DSFKVYCNFT AGGETCIYPD
1660 1670 1680 1690 1700
KKSEGVRLSS WPKEKPGSWY SEFKRGKLLS YLDVEGNSIN MVQMTFLKLL
1710 1720 1730 1740 1750
TASARQNFTY NCHQSTAWYD VLSGSYDKAL RFLGSNDEEM SYENNPHIKA
1760 1770 1780 1790 1800
LYDGCASRKG YEKTVIEINT PKIDQVPIID VMINDFGDQN QKFGFEVGPA

CFLG
Length:1,804
Mass (Da):181,027
Last modified:March 21, 2012 - v2
Checksum:i666A4E0FDCC0BA3B
GO
Isoform 2 (identifier: P20909-2) [UniParc]FASTAAdd to basket

Also known as: +V1b+V2, p6B+8

The sequence of this isoform differs from the canonical sequence as follows:
     259-297: YAPEDIIEYD...VTEETVAQTE → KKKSNYTKKK...ATAKAKLGVQ

Show »
Length:1,816
Mass (Da):182,258
Checksum:i6BFB79E300FC1557
GO
Isoform 3 (identifier: P20909-3) [UniParc]FASTAAdd to basket

Also known as: +V2, p8

The sequence of this isoform differs from the canonical sequence as follows:
     259-297: Missing.

Show »
Length:1,765
Mass (Da):176,505
Checksum:i94FAC45C05007DCA
GO
Isoform 4 (identifier: P20909-4) [UniParc]FASTAAdd to basket

Also known as: +V1a, p6A

The sequence of this isoform differs from the canonical sequence as follows:
     329-413: Missing.

Show »
Length:1,719
Mass (Da):171,370
Checksum:i4B3D6137A5097BFA
GO
Isoform 5 (identifier: P20909-5) [UniParc]FASTAAdd to basket

Also known as: +V1b, p6B

The sequence of this isoform differs from the canonical sequence as follows:
     259-297: YAPEDIIEYD...VTEETVAQTE → KKKSNYTKKK...ATAKAKLGVQ
     329-413: Missing.

Show »
Length:1,731
Mass (Da):172,601
Checksum:iBB53A77411763C20
GO
Isoform 6 (identifier: P20909-6) [UniParc]FASTAAdd to basket

Also known as: -V1-V2, p0

The sequence of this isoform differs from the canonical sequence as follows:
     259-297: Missing.
     329-413: Missing.

Show »
Length:1,680
Mass (Da):166,848
Checksum:i588F418A9DDDF8B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 3941S → A in AAA92358 (PubMed:7721875).Curated
Sequence conflicti394 – 3941S → A in AAA92359 (PubMed:7721875).Curated
Sequence conflicti394 – 3941S → A in AAA92360 (PubMed:7721875).Curated
Sequence conflicti394 – 3941S → A in AAK83570 (PubMed:7721875).Curated
Sequence conflicti1371 – 13711R → G no nucleotide entry (PubMed:3182841).Curated
Sequence conflicti1702 – 17021A → S no nucleotide entry (PubMed:3182841).Curated
Sequence conflicti1743 – 17431E → D no nucleotide entry (PubMed:3182841).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei259 – 29739YAPED…VAQTE → KKKSNYTKKKRTLATNSKKK SKMSTTPKSEKFASKKKKRN QATAKAKLGVQ in isoform 2 and isoform 5. 1 PublicationVSP_042438Add
BLAST
Alternative sequencei259 – 29739Missing in isoform 3 and isoform 6. CuratedVSP_042439Add
BLAST
Alternative sequencei329 – 41385Missing in isoform 4, isoform 5 and isoform 6. CuratedVSP_042440Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012126 Genomic DNA. No translation available.
AABR03013126 Genomic DNA. No translation available.
AABR03014171 Genomic DNA. No translation available.
AABR03015382 Genomic DNA. No translation available.
AABR03015832 Genomic DNA. No translation available.
AABR03016562 Genomic DNA. No translation available.
AABR03017847 Genomic DNA. No translation available.
AABR03017951 Genomic DNA. No translation available.
AABR03018245 Genomic DNA. No translation available.
AABR03019675 Genomic DNA. No translation available.
AABR03023874 Genomic DNA. No translation available.
U20116 Genomic DNA. Translation: AAK83682.1.
U20118 Genomic DNA. Translation: AAK83568.2.
U20118 Genomic DNA. Translation: AAK83569.2.
U20118 Genomic DNA. Translation: AAK83570.2.
U20118 Genomic DNA. Translation: AAK83571.2.
U20118 Genomic DNA. Translation: AAA92358.3.
U20118 Genomic DNA. Translation: AAA92359.3.
U20121 mRNA. Translation: AAA92360.1.
PIRiB31795.
RefSeqiNP_037249.1. NM_013117.1. [P20909-1]
XP_006233272.1. XM_006233210.2. [P20909-2]
UniGeneiRn.260.

Genome annotation databases

EnsembliENSRNOT00000068413; ENSRNOP00000061595; ENSRNOG00000023148. [P20909-1]
GeneIDi25654.
KEGGirno:25654.
UCSCiRGD:2372. rat. [P20909-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012126 Genomic DNA. No translation available.
AABR03013126 Genomic DNA. No translation available.
AABR03014171 Genomic DNA. No translation available.
AABR03015382 Genomic DNA. No translation available.
AABR03015832 Genomic DNA. No translation available.
AABR03016562 Genomic DNA. No translation available.
AABR03017847 Genomic DNA. No translation available.
AABR03017951 Genomic DNA. No translation available.
AABR03018245 Genomic DNA. No translation available.
AABR03019675 Genomic DNA. No translation available.
AABR03023874 Genomic DNA. No translation available.
U20116 Genomic DNA. Translation: AAK83682.1.
U20118 Genomic DNA. Translation: AAK83568.2.
U20118 Genomic DNA. Translation: AAK83569.2.
U20118 Genomic DNA. Translation: AAK83570.2.
U20118 Genomic DNA. Translation: AAK83571.2.
U20118 Genomic DNA. Translation: AAA92358.3.
U20118 Genomic DNA. Translation: AAA92359.3.
U20121 mRNA. Translation: AAA92360.1.
PIRiB31795.
RefSeqiNP_037249.1. NM_013117.1. [P20909-1]
XP_006233272.1. XM_006233210.2. [P20909-2]
UniGeneiRn.260.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP20909. 33 interactions.
STRINGi10116.ENSRNOP00000023794.

PTM databases

PhosphoSiteiP20909.

Proteomic databases

PaxDbiP20909.
PRIDEiP20909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000068413; ENSRNOP00000061595; ENSRNOG00000023148. [P20909-1]
GeneIDi25654.
KEGGirno:25654.
UCSCiRGD:2372. rat. [P20909-1]

Organism-specific databases

CTDi1301.
RGDi2372. Col11a1.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG103137.
InParanoidiP20909.
KOiK19721.
OMAiHPGKEGQ.
OrthoDBiEOG7XPZ4W.
TreeFamiTF323987.

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1650814. Collagen biosynthesis and modifying enzymes.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

NextBioi607535.
PROiP20909.

Gene expression databases

GenevisibleiP20909. RN.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Alternative exon splicing within the amino-terminal nontriple-helical domain of the rat pro-alpha 1(XI) collagen chain generates multiple forms of the mRNA transcript which exhibit tissue-dependent variation."
    Oxford J.T., Doege K.J., Morris N.P.
    J. Biol. Chem. 270:9478-9485(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-556 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6).
    Strain: Sprague-Dawley.
    Tissue: Chondrosarcoma.
  3. "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 1323-1804.
  4. "Structural organization of distinct domains within the non-collagenous N-terminal region of collagen type XI."
    Gregory K.E., Oxford J.T., Chen Y., Gambee J.E., Gygi S.P., Aebersold R., Neame P.J., Mechling D.E., Bachinger H.P., Morris N.P.
    J. Biol. Chem. 275:11498-11506(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION.

Entry informationi

Entry nameiCOBA1_RAT
AccessioniPrimary (citable) accession number: P20909
Secondary accession number(s): F1LSI4
, Q62750, Q63391, Q63392, Q63393, Q8VBY8, Q920Z7, Q920Z8, Q920Z9, Q921A0, Q921A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 21, 2012
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.