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P12111 (CO6A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-3(VI) chain
Gene names
Name:COL6A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Collagen VI acts as a cell-binding protein.

Subunit structure

Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).

Subcellular location

Secretedextracellular spaceextracellular matrix 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.

The N-terminus is blocked.

Involvement in disease

Bethlem myopathy (BM) [MIM:158810]: A benign autosomal dominant proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Ullrich congenital muscular dystrophy (UCMD) [MIM:254090]: UCMD is a congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.19

Sequence similarities

Belongs to the type VI collagen family.

Contains 1 BPTI/Kunitz inhibitor domain.

Contains 5 collagen-like domains.

Contains 1 fibronectin type-III domain.

Contains 12 VWFA domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCollagen
Repeat
Signal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

collagen catabolic process

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

muscle organ development

Traceable author statement PubMed 8782832. Source: ProtInc

   Cellular_componentcollagen type VI

Traceable author statement PubMed 8782832. Source: ProtInc

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from direct assay PubMed 18400749. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12111-1)

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 2 (identifier: P12111-2)

The sequence of this isoform differs from the canonical sequence as follows:
     31-236: Missing.
Isoform 3 (identifier: P12111-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-236: Missing.
     237-437: Missing.
     1429-1443: AVESDAADIVFLIDS → GEMGASEVLLGAFSI
     1444-3177: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P12111-4)

The sequence of this isoform differs from the canonical sequence as follows:
     31-437: Missing.
     633-832: Missing.
Isoform 5 (identifier: P12111-5)

The sequence of this isoform differs from the canonical sequence as follows:
     31-236: Missing.
     1429-1443: AVESDAADIVFLIDS → GEMGASEVLLGAFSI
     1444-3177: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 31773152Collagen alpha-3(VI) chain
PRO_0000005847

Regions

Domain39 – 213175VWFA 1
Domain242 – 419178VWFA 2
Domain445 – 620176VWFA 3
Domain639 – 816178VWFA 4
Domain837 – 1009173VWFA 5
Domain1029 – 1205177VWFA 6
Domain1233 – 1404172VWFA 7
Domain1436 – 1609174VWFA 8
Domain1639 – 1812174VWFA 9
Domain1838 – 2024187VWFA 10
Domain2038 – 209760Collagen-like 1
Domain2104 – 216360Collagen-like 2
Domain2174 – 223360Collagen-like 3
Domain2249 – 230052Collagen-like 4
Domain2314 – 237360Collagen-like 5
Domain2402 – 2581180VWFA 11
Domain2619 – 2815197VWFA 12
Domain2991 – 308595Fibronectin type-III
Domain3112 – 316251BPTI/Kunitz inhibitor
Region26 – 20382013Nonhelical region
Region2039 – 2375337Triple-helical region
Region2376 – 3177802Nonhelical region
Motif2040 – 20423Cell attachment site
Motif2136 – 21383Cell attachment site
Motif2148 – 21503Cell attachment site
Motif2154 – 21563Cell attachment site
Motif2370 – 23723Cell attachment site
Compositional bias2863 – 289836Thr-rich
Compositional bias2908 – 298376Ala-rich

Sites

Site3122 – 31232Reactive bond

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid Probable
Modified residue4331Phosphothreonine Ref.12
Modified residue210014-hydroxyproline
Modified residue210315-hydroxylysine; alternate
Modified residue220614-hydroxyproline
Modified residue220915-hydroxylysine; alternate
Modified residue221215-hydroxylysine; alternate
Modified residue223914-hydroxyproline
Modified residue231614-hydroxyproline
Modified residue231914-hydroxyproline
Modified residue232215-hydroxylysine; alternate
Modified residue233715-hydroxylysine; alternate
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation20791N-linked (GlcNAc...) Ref.11
Glycosylation21031O-linked (Gal...); alternate
Glycosylation22091O-linked (Gal...); alternate
Glycosylation22121O-linked (Gal...); alternate
Glycosylation23221O-linked (Gal...); alternate
Glycosylation23311N-linked (GlcNAc...) Potential
Glycosylation23371O-linked (Gal...); alternate
Glycosylation25581N-linked (GlcNAc...) Potential
Glycosylation26771N-linked (GlcNAc...) Ref.10 Ref.11
Glycosylation28611N-linked (GlcNAc...) Potential
Glycosylation30371N-linked (GlcNAc...) Potential
Disulfide bond2087Interchain By similarity
Disulfide bond3112 ↔ 3162 By similarity
Disulfide bond3121 ↔ 3145 By similarity
Disulfide bond3137 ↔ 3158 By similarity

Natural variations

Alternative sequence31 – 437407Missing in isoform 4.
VSP_045718
Alternative sequence31 – 236206Missing in isoform 2, isoform 3 and isoform 5.
VSP_001172
Alternative sequence237 – 437201Missing in isoform 3.
VSP_043434
Alternative sequence633 – 832200Missing in isoform 4.
VSP_045719
Alternative sequence1429 – 144315AVESD…FLIDS → GEMGASEVLLGAFSI in isoform 3 and isoform 5.
VSP_043435
Alternative sequence1444 – 31771734Missing in isoform 3 and isoform 5.
VSP_043436
Natural variant4111L → V. Ref.19
Corresponds to variant rs113716915 [ dbSNP | Ensembl ].
VAR_058242
Natural variant4911D → H. Ref.19
Corresponds to variant rs112010940 [ dbSNP | Ensembl ].
VAR_058243
Natural variant4921T → S. Ref.19
Corresponds to variant rs113897824 [ dbSNP | Ensembl ].
VAR_058244
Natural variant5381T → M.
Corresponds to variant rs34741387 [ dbSNP | Ensembl ].
VAR_047279
Natural variant6591R → H.
Corresponds to variant rs36092870 [ dbSNP | Ensembl ].
VAR_047280
Natural variant6771R → H in BM; unknown pathological significance. Ref.19 Ref.20
Corresponds to variant rs35227432 [ dbSNP | Ensembl ].
VAR_058245
Natural variant8071A → T. Ref.19
VAR_058246
Natural variant8301A → S. Ref.19
Corresponds to variant rs77181645 [ dbSNP | Ensembl ].
VAR_058247
Natural variant8861V → E.
Corresponds to variant rs9630964 [ dbSNP | Ensembl ].
VAR_047281
Natural variant10141K → E in BM. Ref.19
VAR_058248
Natural variant10641R → Q in UCMD. Ref.19
Corresponds to variant rs112638391 [ dbSNP | Ensembl ].
VAR_058249
Natural variant10881K → Q. Ref.19
Corresponds to variant rs11896521 [ dbSNP | Ensembl ].
VAR_047282
Natural variant13861E → K in BM. Ref.19
Corresponds to variant rs146092501 [ dbSNP | Ensembl ].
VAR_058250
Natural variant13951R → Q in UCMD. Ref.19
Corresponds to variant rs80272723 [ dbSNP | Ensembl ].
VAR_058251
Natural variant14671N → D in BM. Ref.19
VAR_058252
Natural variant15761R → Q. Ref.19 Ref.20
Corresponds to variant rs61729839 [ dbSNP | Ensembl ].
VAR_058253
Natural variant16321R → Q. Ref.19
Corresponds to variant rs111231885 [ dbSNP | Ensembl ].
VAR_058254
Natural variant16741D → N in UCMD. Ref.19
VAR_058255
Natural variant16791G → E in BM. Ref.17 Ref.19
VAR_001910
Natural variant16871P → S. Ref.19
Corresponds to variant rs35273032 [ dbSNP | Ensembl ].
VAR_058256
Natural variant17261L → R in BM. Ref.20
VAR_058257
Natural variant19851V → M in BM. Ref.19
VAR_058258
Natural variant20471G → D in BM. Ref.19
VAR_058259
Natural variant20561G → R in BM. Ref.18
VAR_058260
Natural variant20801G → D in BM. Ref.19
VAR_058261
Natural variant22181P → L. Ref.19
Corresponds to variant rs36117715 [ dbSNP | Ensembl ].
VAR_047283
Natural variant24311D → V. Ref.1 Ref.20
VAR_058262
Natural variant24531E → K. Ref.20
VAR_058263
Natural variant28051N → T.
Corresponds to variant rs35848091 [ dbSNP | Ensembl ].
VAR_047284
Natural variant28311D → H. Ref.17 Ref.19 Ref.20
Corresponds to variant rs36104025 [ dbSNP | Ensembl ].
VAR_001911
Natural variant29271M → T. Ref.1
Corresponds to variant rs6728818 [ dbSNP | Ensembl ].
VAR_047285
Natural variant29411A → V in BM. Ref.19
Corresponds to variant rs11903206 [ dbSNP | Ensembl ].
VAR_058264
Natural variant29881M → V. Ref.1 Ref.20
Corresponds to variant rs11690358 [ dbSNP | Ensembl ].
VAR_047286
Natural variant30121A → P. Ref.1
Corresponds to variant rs2270669 [ dbSNP | Ensembl ].
VAR_047287
Natural variant30691T → I. Ref.20
Corresponds to variant rs1131296 [ dbSNP | Ensembl ].
VAR_047288

Experimental info

Sequence conflict127 – 1282QS → AK in AAB24261. Ref.6
Sequence conflict1371R → L in AAB24261. Ref.6
Sequence conflict3811A → V in BAG65607. Ref.3
Sequence conflict6081F → S in BAG65607. Ref.3
Sequence conflict8851K → E in AAI44596. Ref.5
Sequence conflict8851K → E in AAI50626. Ref.5
Sequence conflict12821V → A in CAA36267. Ref.1
Sequence conflict1353 – 13542DD → VV in CAA36267. Ref.1
Sequence conflict21571P → R in CAA29557. Ref.8
Sequence conflict22571A → R in CAA36267. Ref.1
Sequence conflict22571A → R in M20778. Ref.7
Sequence conflict22871R → P in CAA36267. Ref.1
Sequence conflict22871R → P in M20778. Ref.7
Sequence conflict23571D → R in CAA36267. Ref.1
Sequence conflict23571D → R in M20778. Ref.7
Sequence conflict23671K → R in CAA36267. Ref.1
Sequence conflict23671K → R in M20778. Ref.7
Sequence conflict24411R → T in CAA36267. Ref.1
Sequence conflict29561Missing in CAA36267. Ref.1
Sequence conflict29921S → L in CAA36267. Ref.1

Secondary structure

.............. 3177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 5.
Checksum: 56D54CAC4FBB30AF

FASTA3,177343,669
        10         20         30         40         50         60 
MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI GEEHFQLVRE 

        70         80         90        100        110        120 
FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ EVLSHISNMS YIGGTNQTGK 

       130        140        150        160        170        180 
GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT DGHSKDGLAL PSAELKSADV NVFAIGVEDA 

       190        200        210        220        230        240 
DEGALKEIAS EPLNMHMFNL ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS 

       250        260        270        280        290        300 
ADIIFLIDGS NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS 

       310        320        330        340        350        360 
TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL VLISAGPSSD 

       370        380        390        400        410        420 
EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF TVPEFRSFGD LQEKLLPYIV 

       430        440        450        460        470        480 
GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV DGSSALGLAN FNAIRDFIAK VIQRLEIGQD 

       490        500        510        520        530        540 
LIQVAVAQYA DTVRPEFYFN THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS 

       550        560        570        580        590        600 
AGYRAAEGIP KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS 

       610        620        630        640        650        660 
LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV GKTNFPYVRD 

       670        680        690        700        710        720 
FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS DILGHLRQLQ LQGGSGLNTG 

       730        740        750        760        770        780 
SALSYVYANH FTEAGGSRIR EHVPQLLLLL TAGQSEDSYL QAANALTRAG ILTFCVGASQ 

       790        800        810        820        830        840 
ANKAELEQIA FNPSLVYLMD DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF 

       850        860        870        880        890        900 
LFDGSANLVG QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL 

       910        920        930        940        950        960 
NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG RSSDRVDGPA 

       970        980        990       1000       1010       1020 
SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP KIGDLHPQIV NLLKSVHNGA 

      1030       1040       1050       1060       1070       1080 
PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF VQRVVESLDV GQDRVRVAVV QYSDRTRPEF 

      1090       1100       1110       1120       1130       1140 
YLNSYMNKQD VVNAVRQLTL LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT 

      1150       1160       1170       1180       1190       1200 
ADRSGDDVRN PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV 

      1210       1220       1230       1240       1250       1260 
ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY VRTLIERLVD 

      1270       1280       1290       1300       1310       1320 
YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ RLRPKGGRQI NVGNALEYVS 

      1330       1340       1350       1360       1370       1380 
RNIFKRPLGS RIEEGVPQFL VLISSGKSDD EVDDPAVELK QFGVAPFTIA RNADQEELVK 

      1390       1400       1410       1420       1430       1440 
ISLSPEYVFS VSTFRELPSL EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL 

      1450       1460       1470       1480       1490       1500 
IDSSEGVRPD GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL 

      1510       1520       1530       1540       1550       1560 
DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG KSQDDVSRFA 

      1570       1580       1590       1600       1610       1620 
QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR ELPNIEERIM NSFGPSAATP 

      1630       1640       1650       1660       1670       1680 
APPGVDTPPP SRPEKKKADI VFLLDGSINF RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL 

      1690       1700       1710       1720       1730       1740 
VQYNSDPTDE FFLKDFSTKR QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD 

      1750       1760       1770       1780       1790       1800 
QRVPQIAFVI TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG 

      1810       1820       1830       1840       1850       1860 
NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN VFVAQKGFES 

      1870       1880       1890       1900       1910       1920 
KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA FDFDEYQPEM LEKFRNMRSQ 

      1930       1940       1950       1960       1970       1980 
HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH FTDGADGDLA DLHRASENLR QEGVRALILV 

      1990       2000       2010       2020       2030       2040 
GLERVVNLER LMHLEFGRGF MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR 

      2050       2060       2070       2080       2090       2100 
GDRGPIGSIG PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP 

      2110       2120       2130       2140       2150       2160 
GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD VGIRGDPGNP 

      2170       2180       2190       2200       2210       2220 
GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF GRRGPPGAKG NKGGPGQPGF 

      2230       2240       2250       2260       2270       2280 
EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP RGSGGAAGAP GERGRTGPLG RKGEPGEPGP 

      2290       2300       2310       2320       2330       2340 
KGGIGNRGPR GETGDDGRDG VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR 

      2350       2360       2370       2380       2390       2400 
GRRGNSGPPG IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP 

      2410       2420       2430       2440       2450       2460 
TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY NNEVTTEIRF 

      2470       2480       2490       2500       2510       2520 
ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK RVRNGFLMRK VAVFFSNTPT 

      2530       2540       2550       2560       2570       2580 
RASPQLREAV LKLSDAGITP LFLTRQEDRQ LINALQINNT AVGHALVLPA GRDLTDFLEN 

      2590       2600       2610       2620       2630       2640 
VLTCHVCLDI CNIDPSCGFG SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK 

      2650       2660       2670       2680       2690       2700 
YIAYLVRQLD MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD 

      2710       2720       2730       2740       2750       2760 
FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ QLEEAQRVIL 

      2770       2780       2790       2800       2810       2820 
QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK STELNEEPLM RFGRLLPSFV 

      2830       2840       2850       2860       2870       2880 
SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT 

      2890       2900       2910       2920       2930       2940 
KPVTTTTKPV TTTTKPVTII NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT 

      2950       2960       2970       2980       2990       3000 
AAKPVAAKPA AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI 

      3010       3020       3030       3040       3050       3060 
TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA GQTYHVAVVC 

      3070       3080       3090       3100       3110       3120 
YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS TEPLALTETD ICKLPKDEGT 

      3130       3140       3150       3160       3170 
CRDFILKWYY DPNTKSCARF WYGGCGGNEN KFGSQKECEK VCAPVLAKPG VISVMGT 

« Hide

Isoform 2 [UniParc].

Checksum: BA575D6B63627175
Show »

FASTA2,971321,354
Isoform 3 [UniParc].

Checksum: 9614E1488D7CEE0B
Show »

FASTA1,036113,224
Isoform 4 [UniParc].

Checksum: 952E61BE4F03322C
Show »

FASTA2,570278,203
Isoform 5 [UniParc].

Checksum: 8B77D527A7B34B6D
Show »

FASTA1,237134,707

References

« Hide 'large scale' references
[1]"Mosaic structure of globular domains in the human type VI collagen alpha 3 chain: similarity to von Willebrand factor, fibronectin, actin, salivary proteins and aprotinin type protease inhibitors."
Chu M.-L., Zhang R.-Z., Pan T.-C., Stokes D., Conway D., Kuo H.-J., Glanville R., Mayer U., Mann K., Deutzmann R., Timpl R.
EMBO J. 9:385-393(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS VAL-2431; THR-2927; VAL-2988 AND PRO-3012.
Tissue: Fibroblast.
[2]Chu M.-L.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
Tissue: Uterus.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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).
[6]"The human type VI collagen gene. mRNA and protein variants of the alpha 3 chain generated by alternative splicing of an additional 5-end exon."
Zanussi S., Doliana R., Segat D., Bonaldo P., Colombatti A.
J. Biol. Chem. 267:24082-24089(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-236, ALTERNATIVE SPLICING.
[7]"Amino acid sequence of the triple-helical domain of human collagen type VI."
Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R., Timpl R.
J. Biol. Chem. 263:18601-18606(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2373.
[8]"Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones."
Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C., Bernard M.P., Timpl R.
Eur. J. Biochem. 168:309-317(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2157.
[9]"Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen."
Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D., Mann K., Deutzmann R., Timpl R., Chu M.-L.
Am. J. Hum. Genet. 42:435-445(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2151.
Tissue: Placenta.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2677.
Tissue: Plasma.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2079 AND ASN-2677.
Tissue: Liver.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen."
Arnoux B., Merigeau K., Saludjian P., Norris F., Norris K., Bjoern S., Olsen O., Petersen L., Ducruix A.
J. Mol. Biol. 246:609-617(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3108-3165.
[14]"Structure and multiple conformations of the Kunitz-type domain from human type VI collagen alpha3(VI) chain in solution."
Zweckstetter M., Czisch M., Mayer U., Chu M.-L., Zinth W., Timpl R., Holak T.A.
Structure 4:195-209(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3103-3165.
[15]"Solution structure and backbone dynamics of the human alpha3-chain type VI collagen C-terminal Kunitz domain."
Soerensen M.D., Bjoern S., Norris K., Olsen O., Petersen L., James T.L., Led J.J.
Biochemistry 36:10439-10450(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3108-3165.
[16]"Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy."
Demir E., Sabatelli P., Allamand V., Ferreiro A., Moghadaszadeh B., Makrelouf M., Topaloglu H., Echenne B., Merlini L., Guicheney P.
Am. J. Hum. Genet. 70:1446-1458(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[17]"Missense mutation in a von Willebrand factor type A domain of the alpha 3(VI) collagen gene (COL6A3) in a family with Bethlem myopathy."
Pan T.-C., Zhang R.-Z., Pericak-Vance M.A., Tandan R., Fries T., Stajich J.M., Viles K., Vance J.M., Chu M.-L., Speer M.C.
Hum. Mol. Genet. 7:807-812(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM GLU-1679, VARIANT HIS-2831.
[18]"A novel de novo mutation in the triple helix of the COL6A3 gene in a two-generation Italian family affected by Bethlem myopathy. A diagnostic approach in the mutations' screening of type VI collagen."
Pepe G., Bertini E., Giusti B., Brunelli T., Comeglio P., Saitta B., Merlini L., Chu M.L., Federici G., Abbate R.
Neuromuscul. Disord. 9:264-271(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM ARG-2056.
[19]"Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy."
Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A., Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F., Bonnemann C.G., Flanigan K.M., Bushby K.M.D., Weiss R.B.
J. Med. Genet. 42:108-120(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BM HIS-677; GLU-1014; LYS-1386; ASP-1467; GLU-1679; MET-1985; ASP-2047; ASP-2080 AND VAL-2941, VARIANTS UCMD GLN-1064; GLN-1395 AND ASN-1674, VARIANTS VAL-411; HIS-491; SER-492; THR-807; SER-830; GLN-1088; GLN-1576; GLN-1632; SER-1687; LEU-2218 AND HIS-2831.
[20]"Molecular consequences of dominant Bethlem myopathy collagen VI mutations."
Baker N.L., Moergelin M., Pace R.A., Peat R.A., Adams N.E., Gardner R.J., Rowland L.P., Miller G., De Jonghe P., Ceulemans B., Hannibal M.C., Edwards M., Thompson E.M., Jacobson R., Quinlivan R.C.M., Aftimos S., Kornberg A.J., North K.N., Bateman J.F., Lamande S.R.
Ann. Neurol. 62:390-405(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BM ARG-1726, VARIANTS HIS-677; GLN-1576; VAL-2431; LYS-2453; HIS-2831; VAL-2988 AND ILE-3069.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52022 mRNA. Translation: CAA36267.1.
AK092021 mRNA. Translation: BAG52467.1.
AK304870 mRNA. Translation: BAG65607.1.
AC112715 Genomic DNA. Translation: AAY14906.1.
AC112721 Genomic DNA. Translation: AAY24135.1.
BC144595 mRNA. Translation: AAI44596.1.
BC150625 mRNA. Translation: AAI50626.1.
S49432 mRNA. Translation: AAB24261.1.
M20778 mRNA. No translation available.
X06196 mRNA. Translation: CAA29557.1.
M27449 mRNA. Translation: AAA52057.1.
PIRCGHU3A. A59140.
RefSeqNP_004360.2. NM_004369.3.
NP_476505.3. NM_057164.4.
NP_476506.3. NM_057165.4.
NP_476507.3. NM_057166.4.
NP_476508.2. NM_057167.3.
UniGeneHs.233240.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNTX-ray1.60A3108-3165[»]
1KTHX-ray0.95A3108-3164[»]
1KUNNMR-A3108-3165[»]
2KNTX-ray1.20A3108-3164[»]
ProteinModelPortalP12111.
SMRP12111. Positions 3108-3165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP12111. 4 interactions.
MINTMINT-4053347.
STRING9606.ENSP00000295550.

Chemistry

ChEMBLCHEMBL2364188.

Protein family/group databases

MEROPSI02.968.

PTM databases

PhosphoSiteP12111.

Polymorphism databases

DMDM311033499.

Proteomic databases

PaxDbP12111.
PRIDEP12111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295550; ENSP00000295550; ENSG00000163359. [P12111-1]
ENST00000353578; ENSP00000315873; ENSG00000163359. [P12111-2]
ENST00000392003; ENSP00000375860; ENSG00000163359. [P12111-3]
ENST00000392004; ENSP00000375861; ENSG00000163359. [P12111-5]
ENST00000409809; ENSP00000386844; ENSG00000163359. [P12111-2]
ENST00000472056; ENSP00000418285; ENSG00000163359. [P12111-4]
GeneID1293.
KEGGhsa:1293.
UCSCuc002vwl.2. human. [P12111-1]
uc002vwo.2. human. [P12111-2]
uc002vwr.3. human. [P12111-3]
uc010znj.1. human.

Organism-specific databases

CTD1293.
GeneCardsGC02M238248.
H-InvDBHIX0002952.
HGNCHGNC:2213. COL6A3.
HPAHPA010080.
MIM120250. gene.
158810. phenotype.
254090. phenotype.
neXtProtNX_P12111.
Orphanet610. Bethlem myopathy.
75840. Congenital muscular dystrophy, Ullrich type.
PharmGKBPA26729.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237718.
HOGENOMHOG000015249.
HOVERGENHBG051052.
InParanoidP12111.
KOK06238.
OMAGRHANTK.
OrthoDBEOG7N0C3R.
PhylomeDBP12111.
TreeFamTF337483.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP12111.
BgeeP12111.
CleanExHS_COL6A3.
GenevestigatorP12111.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.40.50.410. 12 hits.
4.10.410.10. 1 hit.
InterProIPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 1 hit.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 11 hits.
[Graphical view]
PRINTSPR00759. BASICPTASE.
SMARTSM00060. FN3. 1 hit.
SM00131. KU. 1 hit.
SM00327. VWA. 12 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF53300. SSF53300. 12 hits.
SSF57362. SSF57362. 1 hit.
PROSITEPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 1 hit.
PS50234. VWFA. 12 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL6A3. human.
EvolutionaryTraceP12111.
GeneWikiCOL6A3.
GenomeRNAi1293.
NextBio5239.
PROP12111.
SOURCESearch...

Entry information

Entry nameCO6A3_HUMAN
AccessionPrimary (citable) accession number: P12111
Secondary accession number(s): A8MT30 expand/collapse secondary AC list , B4E3U5, B7ZMJ7, E9PFQ6, E9PGQ9, Q16501, Q53QF4, Q53QF6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 172 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM