P12111 (CO6A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-3(VI) chain

Gene names

Name:

COL6A3

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	3177 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	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	Secreted › extracellular space › extracellular 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 process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Collagen Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix organization Traceable author statement. Source: Reactome muscle organ development Traceable author statement PubMed 8782832. Source: ProtInc
Cellular_component	collagen type VI Traceable author statement PubMed 8782832. Source: ProtInc endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL sarcolemma Inferred from electronic annotation. Source: Compara transport vesicle Traceable author statement. Source: Reactome
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 3177

3152

Collagen alpha-3(VI) chain

PRO_0000005847

Regions

Domain

39 – 213

175

VWFA 1

Domain

242 – 419

178

VWFA 2

Domain

445 – 620

176

VWFA 3

Domain

639 – 816

178

VWFA 4

Domain

837 – 1009

173

VWFA 5

Domain

1029 – 1205

177

VWFA 6

Domain

1233 – 1404

172

VWFA 7

Domain

1436 – 1609

174

VWFA 8

Domain

1639 – 1812

174

VWFA 9

Domain

1838 – 2024

187

VWFA 10

Domain

2038 – 2097

60

Collagen-like 1

Domain

2104 – 2163

60

Collagen-like 2

Domain

2174 – 2233

60

Collagen-like 3

Domain

2249 – 2300

52

Collagen-like 4

Domain

2314 – 2373

60

Collagen-like 5

Domain

2402 – 2581

180

VWFA 11

Domain

2619 – 2815

197

VWFA 12

Domain

2988 – 3076

89

Fibronectin type-III

Domain

3112 – 3162

51

BPTI/Kunitz inhibitor

Region

26 – 2038

2013

Nonhelical region

Region

2039 – 2375

337

Triple-helical region

Region

2376 – 3177

802

Nonhelical region

Motif

2040 – 2042

3

Cell attachment site

Motif

2136 – 2138

3

Cell attachment site

Motif

2148 – 2150

3

Cell attachment site

Motif

2154 – 2156

3

Cell attachment site

Motif

2370 – 2372

3

Cell attachment site

Compositional bias

2863 – 2898

36

Thr-rich

Compositional bias

2908 – 2983

76

Ala-rich

Sites

Site

3122 – 3123

2

Reactive bond

Amino acid modifications

Modified residue

26

1

Pyrrolidone carboxylic acid Probable

Modified residue

433

1

Phosphothreonine Ref.12

Modified residue

2100

1

4-hydroxyproline

Modified residue

2103

1

5-hydroxylysine; alternate

Modified residue

2206

1

4-hydroxyproline

Modified residue

2209

1

5-hydroxylysine; alternate

Modified residue

2212

1

5-hydroxylysine; alternate

Modified residue

2239

1

4-hydroxyproline

Modified residue

2316

1

4-hydroxyproline

Modified residue

2319

1

4-hydroxyproline

Modified residue

2322

1

5-hydroxylysine; alternate

Modified residue

2337

1

5-hydroxylysine; alternate

Glycosylation

108

1

N-linked (GlcNAc...) Potential

Glycosylation

116

1

N-linked (GlcNAc...) Potential

Glycosylation

202

1

N-linked (GlcNAc...) Potential

Glycosylation

251

1

N-linked (GlcNAc...) Potential

Glycosylation

2079

1

N-linked (GlcNAc...) Ref.11

Glycosylation

2103

1

O-linked (Gal...); alternate

Glycosylation

2209

1

O-linked (Gal...); alternate

Glycosylation

2212

1

O-linked (Gal...); alternate

Glycosylation

2322

1

O-linked (Gal...); alternate

Glycosylation

2331

1

N-linked (GlcNAc...) Potential

Glycosylation

2337

1

O-linked (Gal...); alternate

Glycosylation

2558

1

N-linked (GlcNAc...) Potential

Glycosylation

2677

1

N-linked (GlcNAc...) Ref.10 Ref.11

Glycosylation

2861

1

N-linked (GlcNAc...) Potential

Glycosylation

3037

1

N-linked (GlcNAc...) Potential

Disulfide bond

2087

Interchain By similarity

Disulfide bond

3112 ↔ 3162

By similarity

Disulfide bond

3121 ↔ 3145

By similarity

Disulfide bond

3137 ↔ 3158

By similarity

Natural variations

Alternative sequence

31 – 437

407

Missing in isoform 4.

VSP_045718

Alternative sequence

31 – 236

206

Missing in isoform 2 and isoform 3.

VSP_001172

Alternative sequence

237 – 437

201

Missing in isoform 3.

VSP_043434

Alternative sequence

633 – 832

200

Missing in isoform 4.

VSP_045719

Alternative sequence

1429 – 1443

15

AVESD…FLIDS → GEMGASEVLLGAFSI in isoform 3.

VSP_043435

Alternative sequence

1444 – 3177

1734

Missing in isoform 3.

VSP_043436

Natural variant

411

1

L → V. Ref.19

VAR_058242

Natural variant

491

1

D → H. Ref.19

VAR_058243

Natural variant

492

1

T → S. Ref.19

VAR_058244

Natural variant

538

1

T → M.
Corresponds to variant rs34741387 [ dbSNP | Ensembl ].

VAR_047279

Natural variant

659

1

R → H.
Corresponds to variant rs36092870 [ dbSNP | Ensembl ].

VAR_047280

Natural variant

677

1

R → H in BM; uncertain pathogenicity. Ref.19 Ref.20
Corresponds to variant rs35227432 [ dbSNP | Ensembl ].

VAR_058245

Natural variant

807

1

A → T. Ref.19

VAR_058246

Natural variant

830

1

A → S. Ref.19

VAR_058247

Natural variant

886

1

V → E.
Corresponds to variant rs9630964 [ dbSNP | Ensembl ].

VAR_047281

Natural variant

1014

1

K → E in BM. Ref.19

VAR_058248

Natural variant

1064

1

R → Q in UCMD. Ref.19

VAR_058249

Natural variant

1088

1

K → Q. Ref.19
Corresponds to variant rs11896521 [ dbSNP | Ensembl ].

VAR_047282

Natural variant

1386

1

E → K in BM. Ref.19

VAR_058250

Natural variant

1395

1

R → Q in UCMD. Ref.19

VAR_058251

Natural variant

1467

1

N → D in BM. Ref.19

VAR_058252

Natural variant

1576

1

R → Q. Ref.19 Ref.20

VAR_058253

Natural variant

1632

1

R → Q. Ref.19

VAR_058254

Natural variant

1674

1

D → N in UCMD. Ref.19

VAR_058255

Natural variant

1679

1

G → E in BM. Ref.17 Ref.19

VAR_001910

Natural variant

1687

1

P → S. Ref.19
Corresponds to variant rs35273032 [ dbSNP | Ensembl ].

VAR_058256

Natural variant

1726

1

L → R in BM. Ref.20

VAR_058257

Natural variant

1985

1

V → M in BM. Ref.19

VAR_058258

Natural variant

2047

1

G → D in BM. Ref.19

VAR_058259

Natural variant

2056

1

G → R in BM. Ref.18

VAR_058260

Natural variant

2080

1

G → D in BM. Ref.19

VAR_058261

Natural variant

2218

1

P → L. Ref.19
Corresponds to variant rs36117715 [ dbSNP | Ensembl ].

VAR_047283

Natural variant

2431

1

D → V. Ref.1 Ref.20

VAR_058262

Natural variant

2453

1

E → K. Ref.20

VAR_058263

Natural variant

2805

1

N → T.
Corresponds to variant rs35848091 [ dbSNP | Ensembl ].

VAR_047284

Natural variant

2831

1

D → H. Ref.17 Ref.19 Ref.20
Corresponds to variant rs36104025 [ dbSNP | Ensembl ].

VAR_001911

Natural variant

2927

1

M → T. Ref.1
Corresponds to variant rs6728818 [ dbSNP | Ensembl ].

VAR_047285

Natural variant

2941

1

A → V in BM. Ref.19
Corresponds to variant rs11903206 [ dbSNP | Ensembl ].

VAR_058264

Natural variant

2988

1

M → V. Ref.1 Ref.20
Corresponds to variant rs11690358 [ dbSNP | Ensembl ].

VAR_047286

Natural variant

3012

1

A → P. Ref.1
Corresponds to variant rs2270669 [ dbSNP | Ensembl ].

VAR_047287

Natural variant

3069

1

T → I. Ref.20
Corresponds to variant rs1131296 [ dbSNP | Ensembl ].

VAR_047288

Experimental info

Sequence conflict

127 – 128

2

QS → AK in AAB24261. Ref.6

Sequence conflict

137

1

R → L in AAB24261. Ref.6

Sequence conflict

885

1

K → E in AAI44596. Ref.5

Sequence conflict

885

1

K → E in AAI50626. Ref.5

Sequence conflict

1282

1

V → A in CAA36267. Ref.1

Sequence conflict

1353 – 1354

2

DD → VV in CAA36267. Ref.1

Sequence conflict

2157

1

P → R in CAA29557. Ref.8

Sequence conflict

2257

1

A → R in CAA36267. Ref.1

Sequence conflict

2257

1

A → R in M20778. Ref.7

Sequence conflict

2287

1

R → P in CAA36267. Ref.1

Sequence conflict

2287

1

R → P in M20778. Ref.7

Sequence conflict

2357

1

D → R in CAA36267. Ref.1

Sequence conflict

2357

1

D → R in M20778. Ref.7

Sequence conflict

2367

1

K → R in CAA36267. Ref.1

Sequence conflict

2367

1

K → R in M20778. Ref.7

Sequence conflict

2441

1

R → T in CAA36267. Ref.1

Sequence conflict

2956

1

Missing in CAA36267. Ref.1

Sequence conflict

2992

1

S → L in CAA36267. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3177

Helix Strand Turn

Details...

Helix

3110 – 3113

4

Beta strand

3120 – 3122

3

Beta strand

3125 – 3131

7

Turn

3132 – 3135

4

Beta strand

3136 – 3142

7

Beta strand

3144 – 3146

3

Beta strand

3152 – 3154

3

Helix

3155 – 3162

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2010. Version 5. Checksum: 56D54CAC4FBB30AF	FASTA	3,177	343,669
	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
	Isoform 2 [UniParc]. Checksum: BA575D6B63627175	FASTA	2,971	321,354
	10 20 30 40 50 60 MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA AQDSADIIFL IDGSNNTGSV NFAVILDFLV 70 80 90 100 110 120 NLLEKLPIGT QQIRVGVVQF SDEPRTMFSL DTYSTKAQVL GAVKALGFAG GELANIGLAL 130 140 150 160 170 180 DFVVENHFTR AGGSRVEEGV PQVLVLISAG PSSDEIRYGV VALKQASVFS FGLGAQAASR 190 200 210 220 230 240 AELQHIATDD NLVFTVPEFR SFGDLQEKLL PYIVGVAQRH IVLKPPTIVT QVIEVNKRDI 250 260 270 280 290 300 VFLVDGSSAL GLANFNAIRD FIAKVIQRLE IGQDLIQVAV AQYADTVRPE FYFNTHPTKR 310 320 330 340 350 360 EVITAVRKMK PLDGSALYTG SALDFVRNNL FTSSAGYRAA EGIPKLLVLI TGGKSLDEIS 370 380 390 400 410 420 QPAQELKRSS IMAFAIGNKG ADQAELEEIA FDSSLVFIPA EFRAAPLQGM LPGLLAPLRT 430 440 450 460 470 480 LSGTPEVHSN KRDIIFLLDG SANVGKTNFP YVRDFVMNLV NSLDIGNDNI RVGLVQFSDT 490 500 510 520 530 540 PVTEFSLNTY QTKSDILGHL RQLQLQGGSG LNTGSALSYV YANHFTEAGG SRIREHVPQL 550 560 570 580 590 600 LLLLTAGQSE DSYLQAANAL TRAGILTFCV GASQANKAEL EQIAFNPSLV YLMDDFSSLP 610 620 630 640 650 660 ALPQQLIQPL TTYVSGGVEE VPLAQPESKR DILFLFDGSA NLVGQFPVVR DFLYKIIDEL 670 680 690 700 710 720 NVKPEGTRIA VAQYSDDVKV ESRFDEHQSK PEILNLVKRM KIKTGKALNL GYALDYAQRY 730 740 750 760 770 780 IFVKSAGSRI EDGVLQFLVL LVAGRSSDRV DGPASNLKQS GVVPFIFQAK NADPAELEQI 790 800 810 820 830 840 VLSPAFILAA ESLPKIGDLH PQIVNLLKSV HNGAPAPVSG EKDVVFLLDG SEGVRSGFPL 850 860 870 880 890 900 LKEFVQRVVE SLDVGQDRVR VAVVQYSDRT RPEFYLNSYM NKQDVVNAVR QLTLLGGPTP 910 920 930 940 950 960 NTGAALEFVL RNILVSSAGS RITEGVPQLL IVLTADRSGD DVRNPSVVVK RGGAVPIGIG 970 980 990 1000 1010 1020 IGNADITEMQ TISFIPDFAV AIPTFRQLGT VQQVISERVT QLTREELSRL QPVLQPLPSP 1030 1040 1050 1060 1070 1080 GVGGKRDVVF LIDGSQSAGP EFQYVRTLIE RLVDYLDVGF DTTRVAVIQF SDDPKVEFLL 1090 1100 1110 1120 1130 1140 NAHSSKDEVQ NAVQRLRPKG GRQINVGNAL EYVSRNIFKR PLGSRIEEGV PQFLVLISSG 1150 1160 1170 1180 1190 1200 KSDDEVDDPA VELKQFGVAP FTIARNADQE ELVKISLSPE YVFSVSTFRE LPSLEQKLLT 1210 1220 1230 1240 1250 1260 PITTLTSEQI QKLLASTRYP PPAVESDAAD IVFLIDSSEG VRPDGFAHIR DFVSRIVRRL 1270 1280 1290 1300 1310 1320 NIGPSKVRVG VVQFSNDVFP EFYLKTYRSQ APVLDAIRRL RLRGGSPLNT GKALEFVARN 1330 1340 1350 1360 1370 1380 LFVKSAGSRI EDGVPQHLVL VLGGKSQDDV SRFAQVIRSS GIVSLGVGDR NIDRTELQTI 1390 1400 1410 1420 1430 1440 TNDPRLVFTV REFRELPNIE ERIMNSFGPS AATPAPPGVD TPPPSRPEKK KADIVFLLDG 1450 1460 1470 1480 1490 1500 SINFRRDSFQ EVLRFVSEIV DTVYEDGDSI QVGLVQYNSD PTDEFFLKDF STKRQIIDAI 1510 1520 1530 1540 1550 1560 NKVVYKGGRH ANTKVGLEHL RVNHFVPEAG SRLDQRVPQI AFVITGGKSV EDAQDVSLAL 1570 1580 1590 1600 1610 1620 TQRGVKVFAV GVRNIDSEEV GKIASNSATA FRVGNVQELS ELSEQVLETL HDAMHETLCP 1630 1640 1650 1660 1670 1680 GVTDAAKACN LDVILGFDGS RDQNVFVAQK GFESKVDAIL NRISQMHRVS CSGGRSPTVR 1690 1700 1710 1720 1730 1740 VSVVANTPSG PVEAFDFDEY QPEMLEKFRN MRSQHPYVLT EDTLKVYLNK FRQSSPDSVK 1750 1760 1770 1780 1790 1800 VVIHFTDGAD GDLADLHRAS ENLRQEGVRA LILVGLERVV NLERLMHLEF GRGFMYDRPL 1810 1820 1830 1840 1850 1860 RLNLLDLDYE LAEQLDNIAE KACCGVPCKC SGQRGDRGPI GSIGPKGIPG EDGYRGYPGD 1870 1880 1890 1900 1910 1920 EGGPGERGPP GVNGTQGFQG CPGQRGVKGS RGFPGEKGEV GEIGLDGLDG EDGDKGLPGS 1930 1940 1950 1960 1970 1980 SGEKGNPGRR GDKGPRGEKG ERGDVGIRGD PGNPGQDSQE RGPKGETGDL GPMGVPGRDG 1990 2000 2010 2020 2030 2040 VPGGPGETGK NGGFGRRGPP GAKGNKGGPG QPGFEGEQGT RGAQGPAGPA GPPGLIGEQG 2050 2060 2070 2080 2090 2100 ISGPRGSGGA AGAPGERGRT GPLGRKGEPG EPGPKGGIGN RGPRGETGDD GRDGVGSEGR 2110 2120 2130 2140 2150 2160 RGKKGERGFP GYPGPKGNPG EPGLNGTTGP KGIRGRRGNS GPPGIVGQKG DPGYPGPAGP 2170 2180 2190 2200 2210 2220 KGNRGDSIDQ CALIQSIKDK CPCCYGPLEC PVFPTELAFA LDTSEGVNQD TFGRMRDVVL 2230 2240 2250 2260 2270 2280 SIVNDLTIAE SNCPRGARVA VVTYNNEVTT EIRFADSKRK SVLLDKIKNL QVALTSKQQS 2290 2300 2310 2320 2330 2340 LETAMSFVAR NTFKRVRNGF LMRKVAVFFS NTPTRASPQL REAVLKLSDA GITPLFLTRQ 2350 2360 2370 2380 2390 2400 EDRQLINALQ INNTAVGHAL VLPAGRDLTD FLENVLTCHV CLDICNIDPS CGFGSWRPSF 2410 2420 2430 2440 2450 2460 RDRRAAGSDV DIDMAFILDS AETTTLFQFN EMKKYIAYLV RQLDMSPDPK ASQHFARVAV 2470 2480 2490 2500 2510 2520 VQHAPSESVD NASMPPVKVE FSLTDYGSKE KLVDFLSRGM TQLQGTRALG SAIEYTIENV 2530 2540 2550 2560 2570 2580 FESAPNPRDL KIVVLMLTGE VPEQQLEEAQ RVILQAKCKG YFFVVLGIGR KVNIKEVYTF 2590 2600 2610 2620 2630 2640 ASEPNDVFFK LVDKSTELNE EPLMRFGRLL PSFVSSENAF YLSPDIRKQC DWFQGDQPTK 2650 2660 2670 2680 2690 2700 NLVKFGHKQV NVPNNVTSSP TSNPVTTTKP VTTTKPVTTT TKPVTTTTKP VTIINQPSVK 2710 2720 2730 2740 2750 2760 PAAAKPAPAK PVAAKPVATK MATVRPPVAV KPATAAKPVA AKPAAVRPPA AAAAKPVATK 2770 2780 2790 2800 2810 2820 PEVPRPQAAK PAATKPATTK PMVKMSREVQ VFEITENSAK LHWERAEPPG PYFYDLTVTS 2830 2840 2850 2860 2870 2880 AHDQSLVLKQ NLTVTDRVIG GLLAGQTYHV AVVCYLRSQV RATYHGSFST KKSQPPPPQP 2890 2900 2910 2920 2930 2940 ARSASSSTIN LMVSTEPLAL TETDICKLPK DEGTCRDFIL KWYYDPNTKS CARFWYGGCG 2950 2960 2970 GNENKFGSQK ECEKVCAPVL AKPGVISVMG T
	Isoform 3 [UniParc]. Checksum: 9614E1488D7CEE0B	FASTA	1,036	113,224
	10 20 30 40 50 60 MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA VIEVNKRDIV FLVDGSSALG LANFNAIRDF 70 80 90 100 110 120 IAKVIQRLEI GQDLIQVAVA QYADTVRPEF YFNTHPTKRE VITAVRKMKP LDGSALYTGS 130 140 150 160 170 180 ALDFVRNNLF TSSAGYRAAE GIPKLLVLIT GGKSLDEISQ PAQELKRSSI MAFAIGNKGA 190 200 210 220 230 240 DQAELEEIAF DSSLVFIPAE FRAAPLQGML PGLLAPLRTL SGTPEVHSNK RDIIFLLDGS 250 260 270 280 290 300 ANVGKTNFPY VRDFVMNLVN SLDIGNDNIR VGLVQFSDTP VTEFSLNTYQ TKSDILGHLR 310 320 330 340 350 360 QLQLQGGSGL NTGSALSYVY ANHFTEAGGS RIREHVPQLL LLLTAGQSED SYLQAANALT 370 380 390 400 410 420 RAGILTFCVG ASQANKAELE QIAFNPSLVY LMDDFSSLPA LPQQLIQPLT TYVSGGVEEV 430 440 450 460 470 480 PLAQPESKRD ILFLFDGSAN LVGQFPVVRD FLYKIIDELN VKPEGTRIAV AQYSDDVKVE 490 500 510 520 530 540 SRFDEHQSKP EILNLVKRMK IKTGKALNLG YALDYAQRYI FVKSAGSRIE DGVLQFLVLL 550 560 570 580 590 600 VAGRSSDRVD GPASNLKQSG VVPFIFQAKN ADPAELEQIV LSPAFILAAE SLPKIGDLHP 610 620 630 640 650 660 QIVNLLKSVH NGAPAPVSGE KDVVFLLDGS EGVRSGFPLL KEFVQRVVES LDVGQDRVRV 670 680 690 700 710 720 AVVQYSDRTR PEFYLNSYMN KQDVVNAVRQ LTLLGGPTPN TGAALEFVLR NILVSSAGSR 730 740 750 760 770 780 ITEGVPQLLI VLTADRSGDD VRNPSVVVKR GGAVPIGIGI GNADITEMQT ISFIPDFAVA 790 800 810 820 830 840 IPTFRQLGTV QQVISERVTQ LTREELSRLQ PVLQPLPSPG VGGKRDVVFL IDGSQSAGPE 850 860 870 880 890 900 FQYVRTLIER LVDYLDVGFD TTRVAVIQFS DDPKVEFLLN AHSSKDEVQN AVQRLRPKGG 910 920 930 940 950 960 RQINVGNALE YVSRNIFKRP LGSRIEEGVP QFLVLISSGK SDDEVDDPAV ELKQFGVAPF 970 980 990 1000 1010 1020 TIARNADQEE LVKISLSPEY VFSVSTFREL PSLEQKLLTP ITTLTSEQIQ KLLASTRYPP 1030 PGEMGASEVL LGAFSI
	Isoform 4 [UniParc]. Checksum: 952E61BE4F03322C	FASTA	2,570	278,203
	10 20 30 40 50 60 MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA VIEVNKRDIV FLVDGSSALG LANFNAIRDF 70 80 90 100 110 120 IAKVIQRLEI GQDLIQVAVA QYADTVRPEF YFNTHPTKRE VITAVRKMKP LDGSALYTGS 130 140 150 160 170 180 ALDFVRNNLF TSSAGYRAAE GIPKLLVLIT GGKSLDEISQ PAQELKRSSI MAFAIGNKGA 190 200 210 220 230 240 DQAELEEIAF DSSLVFIPAE FRAAPLQGML PGLLAPLRTL SGTPEESKRD ILFLFDGSAN 250 260 270 280 290 300 LVGQFPVVRD FLYKIIDELN VKPEGTRIAV AQYSDDVKVE SRFDEHQSKP EILNLVKRMK 310 320 330 340 350 360 IKTGKALNLG YALDYAQRYI FVKSAGSRIE DGVLQFLVLL VAGRSSDRVD GPASNLKQSG 370 380 390 400 410 420 VVPFIFQAKN ADPAELEQIV LSPAFILAAE SLPKIGDLHP QIVNLLKSVH NGAPAPVSGE 430 440 450 460 470 480 KDVVFLLDGS EGVRSGFPLL KEFVQRVVES LDVGQDRVRV AVVQYSDRTR PEFYLNSYMN 490 500 510 520 530 540 KQDVVNAVRQ LTLLGGPTPN TGAALEFVLR NILVSSAGSR ITEGVPQLLI VLTADRSGDD 550 560 570 580 590 600 VRNPSVVVKR GGAVPIGIGI GNADITEMQT ISFIPDFAVA IPTFRQLGTV QQVISERVTQ 610 620 630 640 650 660 LTREELSRLQ PVLQPLPSPG VGGKRDVVFL IDGSQSAGPE FQYVRTLIER LVDYLDVGFD 670 680 690 700 710 720 TTRVAVIQFS DDPKVEFLLN AHSSKDEVQN AVQRLRPKGG RQINVGNALE YVSRNIFKRP 730 740 750 760 770 780 LGSRIEEGVP QFLVLISSGK SDDEVDDPAV ELKQFGVAPF TIARNADQEE LVKISLSPEY 790 800 810 820 830 840 VFSVSTFREL PSLEQKLLTP ITTLTSEQIQ KLLASTRYPP PAVESDAADI VFLIDSSEGV 850 860 870 880 890 900 RPDGFAHIRD FVSRIVRRLN IGPSKVRVGV VQFSNDVFPE FYLKTYRSQA PVLDAIRRLR 910 920 930 940 950 960 LRGGSPLNTG KALEFVARNL FVKSAGSRIE DGVPQHLVLV LGGKSQDDVS RFAQVIRSSG 970 980 990 1000 1010 1020 IVSLGVGDRN IDRTELQTIT NDPRLVFTVR EFRELPNIEE RIMNSFGPSA ATPAPPGVDT 1030 1040 1050 1060 1070 1080 PPPSRPEKKK ADIVFLLDGS INFRRDSFQE VLRFVSEIVD TVYEDGDSIQ VGLVQYNSDP 1090 1100 1110 1120 1130 1140 TDEFFLKDFS TKRQIIDAIN KVVYKGGRHA NTKVGLEHLR VNHFVPEAGS RLDQRVPQIA 1150 1160 1170 1180 1190 1200 FVITGGKSVE DAQDVSLALT QRGVKVFAVG VRNIDSEEVG KIASNSATAF RVGNVQELSE 1210 1220 1230 1240 1250 1260 LSEQVLETLH DAMHETLCPG VTDAAKACNL DVILGFDGSR DQNVFVAQKG FESKVDAILN 1270 1280 1290 1300 1310 1320 RISQMHRVSC SGGRSPTVRV SVVANTPSGP VEAFDFDEYQ PEMLEKFRNM RSQHPYVLTE 1330 1340 1350 1360 1370 1380 DTLKVYLNKF RQSSPDSVKV VIHFTDGADG DLADLHRASE NLRQEGVRAL ILVGLERVVN 1390 1400 1410 1420 1430 1440 LERLMHLEFG RGFMYDRPLR LNLLDLDYEL AEQLDNIAEK ACCGVPCKCS GQRGDRGPIG 1450 1460 1470 1480 1490 1500 SIGPKGIPGE DGYRGYPGDE GGPGERGPPG VNGTQGFQGC PGQRGVKGSR GFPGEKGEVG 1510 1520 1530 1540 1550 1560 EIGLDGLDGE DGDKGLPGSS GEKGNPGRRG DKGPRGEKGE RGDVGIRGDP GNPGQDSQER 1570 1580 1590 1600 1610 1620 GPKGETGDLG PMGVPGRDGV PGGPGETGKN GGFGRRGPPG AKGNKGGPGQ PGFEGEQGTR 1630 1640 1650 1660 1670 1680 GAQGPAGPAG PPGLIGEQGI SGPRGSGGAA GAPGERGRTG PLGRKGEPGE PGPKGGIGNR 1690 1700 1710 1720 1730 1740 GPRGETGDDG RDGVGSEGRR GKKGERGFPG YPGPKGNPGE PGLNGTTGPK GIRGRRGNSG 1750 1760 1770 1780 1790 1800 PPGIVGQKGD PGYPGPAGPK GNRGDSIDQC ALIQSIKDKC PCCYGPLECP VFPTELAFAL 1810 1820 1830 1840 1850 1860 DTSEGVNQDT FGRMRDVVLS IVNDLTIAES NCPRGARVAV VTYNNEVTTE IRFADSKRKS 1870 1880 1890 1900 1910 1920 VLLDKIKNLQ VALTSKQQSL ETAMSFVARN TFKRVRNGFL MRKVAVFFSN TPTRASPQLR 1930 1940 1950 1960 1970 1980 EAVLKLSDAG ITPLFLTRQE DRQLINALQI NNTAVGHALV LPAGRDLTDF LENVLTCHVC 1990 2000 2010 2020 2030 2040 LDICNIDPSC GFGSWRPSFR DRRAAGSDVD IDMAFILDSA ETTTLFQFNE MKKYIAYLVR 2050 2060 2070 2080 2090 2100 QLDMSPDPKA SQHFARVAVV QHAPSESVDN ASMPPVKVEF SLTDYGSKEK LVDFLSRGMT 2110 2120 2130 2140 2150 2160 QLQGTRALGS AIEYTIENVF ESAPNPRDLK IVVLMLTGEV PEQQLEEAQR VILQAKCKGY 2170 2180 2190 2200 2210 2220 FFVVLGIGRK VNIKEVYTFA SEPNDVFFKL VDKSTELNEE PLMRFGRLLP SFVSSENAFY 2230 2240 2250 2260 2270 2280 LSPDIRKQCD WFQGDQPTKN LVKFGHKQVN VPNNVTSSPT SNPVTTTKPV TTTKPVTTTT 2290 2300 2310 2320 2330 2340 KPVTTTTKPV TIINQPSVKP AAAKPAPAKP VAAKPVATKM ATVRPPVAVK PATAAKPVAA 2350 2360 2370 2380 2390 2400 KPAAVRPPAA AAAKPVATKP EVPRPQAAKP AATKPATTKP MVKMSREVQV FEITENSAKL 2410 2420 2430 2440 2450 2460 HWERAEPPGP YFYDLTVTSA HDQSLVLKQN LTVTDRVIGG LLAGQTYHVA VVCYLRSQVR 2470 2480 2490 2500 2510 2520 ATYHGSFSTK KSQPPPPQPA RSASSSTINL MVSTEPLALT ETDICKLPKD EGTCRDFILK 2530 2540 2550 2560 2570 WYYDPNTKSC ARFWYGGCGG NENKFGSQKE CEKVCAPVLA KPGVISVMGT

References

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[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. , 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] (ISOFORM 3).
[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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52022 mRNA. Translation: CAA36267.1.
AK092021 mRNA. Translation: BAG52467.1.
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.

IPI

IPI00022200.
IPI00072917.
IPI00220701.
IPI00853061.
IPI00946286.

PIR

CGHU3A. A59140.

RefSeq

NP_004360.2. NM_004369.3.
NP_476505.3. NM_057164.4.
NP_476507.3. NM_057166.4.
NP_476508.2. NM_057167.3.

UniGene

Hs.233240.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KNT	X-ray	1.60	A	3108-3165	[»]
1KTH	X-ray	0.95	A	3108-3164	[»]
1KUN	NMR	-	A	3108-3165	[»]
2KNT	X-ray	1.20	A	3108-3164	[»]

ProteinModelPortal

P12111.

SMR

P12111. Positions 3108-3165.

ModBase

Search...

Protein-protein interaction databases

IntAct

P12111. 3 interactions.

MINT

MINT-4053347.

STRING

9606.ENSP00000295550.

Protein family/group databases

MEROPS

I02.968.

PTM databases

PhosphoSite

P12111.

Polymorphism databases

DMDM

311033499.

Proteomic databases

PaxDb

P12111.

PRIDE

P12111.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295550; ENSP00000295550; ENSG00000163359.
ENST00000353578; ENSP00000315873; ENSG00000163359.
ENST00000392003; ENSP00000375860; ENSG00000163359.
ENST00000409809; ENSP00000386844; ENSG00000163359.
ENST00000472056; ENSP00000418285; ENSG00000163359.

GeneID

1293.

KEGG

hsa:1293.

UCSC

uc002vwl.2. human.
uc002vwo.2. human.

Organism-specific databases

CTD

1293.

GeneCards

GC02M238248.

H-InvDB

HIX0002952.

HGNC

HGNC:2213. COL6A3.

HPA

HPA010080.

MIM

120250. gene.
158810. phenotype.
254090. phenotype.

neXtProt

NX_P12111.

Orphanet

610. Bethlem myopathy.
75840. Congenital muscular dystrophy, Ullrich type.

PharmGKB

PA26729.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG237718.

HOGENOM

HOG000015249.

HOVERGEN

HBG051052.

InParanoid

P12111.

KO

K06238.

OMA

GRHANTK.

OrthoDB

EOG4HT8R9.

PhylomeDB

P12111.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P12111.

Bgee

P12111.

CleanEx

HS_COL6A3.

Genevestigator

P12111.

GermOnline

ENSG00000163359. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
4.10.410.10. 1 hit.

InterPro

IPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF01391. Collagen. 1 hit.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 11 hits.
[Graphical view]

PRINTS

PR00759. BASICPTASE.

SMART

SM00060. FN3. 1 hit.
SM00131. KU. 1 hit.
SM00327. VWA. 12 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 1 hit.
SSF57362. Prot_inh_Kunz-m. 1 hit.

PROSITE

PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 1 hit.
PS50234. VWFA. 12 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

COL6A3. human.

EvolutionaryTrace

P12111.

GenomeRNAi

1293.

NextBio

5239.

SOURCE

Search...

Entry information

Entry name

CO6A3_HUMAN

Accession

Primary (citable) accession number: P12111
Secondary accession number(s): A8MT30 , B7ZMJ7, E9PFQ6, Q16501, Q53QF4, Q53QF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 161 of the entry and version 5 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.