Reviewed, UniProtKB/Swiss-Prot Q8CIZ8 (VWF_MOUSE)

Names and origin

Protein names

Recommended name:
    von Willebrand factor
      Short name=vWF
Cleaved into the following chain:
    1- Recommended name:
            von Willebrand antigen 2
        Alternative name(s):
            von Willebrand antigen II

Gene names

Name:

Vwf

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	2813 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	Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma By similarity. UniProtKB P04275
Subunit structure	Multimeric. Interacts with F8 By similarity.
Subcellular location	Secreted By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Localized to storage granules By similarity.
Tissue specificity	Plasma. Expressed in liver. Ref.7
Domain	The von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules By similarity.
Post-translational modification	All cysteine residues are involved in intrachain or interchain disulfide bonds By similarity. UniProtKB P04275 N- and O-glycosylated By similarity.
Sequence similarities	Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 1 pacifastin repeat. Contains 4 TIL (trypsin inhibitory-like) domains. Contains 3 VWFA domains. Contains 3 VWFC domains. Contains 4 VWFD domains.

Ontologies

Keywords
Biological process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell-substrate adhesion Inferred from sequence or structural similarity. Source: UniProtKB liver development Inferred from mutant phenotype. Source: MGI placenta development Inferred from mutant phenotype. Source: MGI platelet activation Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Weibel-Palade body Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB external side of plasma membrane Inferred from direct assay. Source: MGI proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chaperone binding Inferred from sequence or structural similarity. Source: UniProtKB collagen binding Inferred from sequence or structural similarity. Source: UniProtKB glycoprotein binding Inferred from sequence or structural similarity. Source: UniProtKB immunoglobulin binding Inferred from sequence or structural similarity. Source: UniProtKB integrin binding Inferred from sequence or structural similarity. Source: UniProtKB protease binding Inferred from sequence or structural similarity. Source: UniProtKB protein N-terminus binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.7 (identifier: Q8CIZ8-1)

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: Q8CIZ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     387-402: ECLVTGQSHFKSFDNR → RLGTFSPFLPVLCGEV
     403-2813: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

By similarity UniProtKB P04275

Chain

23 – 763

741

von Willebrand antigen 2 UniProtKB P04275

PRO_0000022684

Chain

764 – 2813

2050

von Willebrand factor UniProtKB P04275

PRO_0000022685

Regions

Domain

34 – 240

207

VWFD 1

Domain

295 – 348

54

TIL 1

Domain

387 – 598

212

VWFD 2

Domain

652 – 707

56

TIL 2

Domain

804 – 827

24

TIL 3

Repeat

835 – 873

39

Pacifastin

Domain

866 – 1074

209

VWFD 3

Domain

1146 – 1196

51

TIL 4

Domain

1277 – 1453

177

VWFA 1; binding site for platelet glycoprotein Ib Ref.7

Domain

1498 – 1665

168

VWFA 2

Domain

1691 – 1871

181

VWFA 3; principal binding site for collagens type I and III Ref.7

Domain

1949 – 2153

205

VWFD 4

Domain

2255 – 2328

74

VWFC 1

Domain

2429 – 2495

67

VWFC 2

Domain

2580 – 2645

66

VWFC 3

Domain

2724 – 2812

89

CTCK

Region

764 – 787

24

Amino-terminal

Region

788 – 833

46

E1

Region

826 – 853

28

CX

Region

2216 – 2261

46

E2

Motif

2507 – 2509

3

Cell attachment site By similarity UniProtKB P04275

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

156

1

N-linked (GlcNAc...) Potential

Glycosylation

666

1

N-linked (GlcNAc...) Potential

Glycosylation

857

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

1005

1

N-linked (GlcNAc...) Potential

Glycosylation

1147

1

N-linked (GlcNAc...); atypical By similarity UniProtKB P04275

Glycosylation

1231

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

1248

1

O-linked (GalNAc...) By similarity

Glycosylation

1255

1

O-linked (GalNAc...) By similarity

Glycosylation

1256

1

O-linked (GalNAc...) By similarity

Glycosylation

1468

1

O-linked (GalNAc...) By similarity

Glycosylation

1477

1

O-linked (GalNAc...) By similarity

Glycosylation

1486

1

O-linked (GalNAc...) By similarity

Glycosylation

1515

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

1574

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

1679

1

O-linked (GalNAc...) By similarity

Glycosylation

2223

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2290

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2298

1

O-linked (GalNAc...) By similarity

Glycosylation

2400

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2546

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2585

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2790

1

N-linked (GlcNAc...) By similarity UniProtKB P04275

Glycosylation

2810

1

N-linked (GlcNAc...) Potential

Disulfide bond

767 ↔ 808

By similarity UniProtKB P04275

Disulfide bond

776 ↔ 804

By similarity UniProtKB P04275

Disulfide bond

810 ↔ 821

By similarity UniProtKB P04275

Disulfide bond

889 ↔ 1031

By similarity UniProtKB P04275

Disulfide bond

898 ↔ 993

By similarity UniProtKB P04275

Disulfide bond

914 ↔ 921

By similarity UniProtKB P04275

Disulfide bond

? ↔ 996

By similarity UniProtKB P04275

Disulfide bond

1060 ↔ 1084

By similarity UniProtKB P04275

Disulfide bond

1071 ↔ 1111

By similarity UniProtKB P04275

Disulfide bond

1089 ↔ 1091

By similarity UniProtKB P04275

Disulfide bond

1126 ↔ 1130

By similarity UniProtKB P04275

Disulfide bond

1149 ↔ 1169

By similarity UniProtKB P04275

Disulfide bond

1153 ↔ 1165

By similarity UniProtKB P04275

Disulfide bond

1196 ↔ 1199

By similarity UniProtKB P04275

Disulfide bond

1234 ↔ 1237

By similarity UniProtKB P04275

Disulfide bond

1272 ↔ 1458

By similarity UniProtKB P04275

Disulfide bond

1669 ↔ 1670

By similarity UniProtKB P04275

Disulfide bond

1686 ↔ 1872

By similarity UniProtKB P04275

Disulfide bond

1879 ↔ 1904

By similarity UniProtKB P04275

Disulfide bond

1899 ↔ 1940

Or C-1899 with C-1942 By similarity UniProtKB P04275

Disulfide bond

1927 ↔ 2088

By similarity UniProtKB P04275

Disulfide bond

1950 ↔ 2085

By similarity UniProtKB P04275

Disulfide bond

1972 ↔ 2123

By similarity UniProtKB P04275

Disulfide bond

1993 ↔ 2001

By similarity UniProtKB P04275

Disulfide bond

2724 ↔ 2774

By similarity UniProtKB P04275

Disulfide bond

2739 ↔ 2788

By similarity UniProtKB P04275

Disulfide bond

2750 ↔ 2804

By similarity UniProtKB P04275

Disulfide bond

2754 ↔ 2806

By similarity UniProtKB P04275

Disulfide bond

? ↔ 2811

By similarity UniProtKB P04275

Cross-link

1720

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence

387 – 402

16

ECLVT…SFDNR → RLGTFSPFLPVLCGEV in isoform 2.

VSP_051618

Alternative sequence

403 – 2813

2411

Missing in isoform 2.

VSP_051619

Experimental info

Mutagenesis

1205

1

R → H: Accelerated clearance of VWF from blood plasma. Ref.7

Sequence conflict

103

1

M → T in AAP41950. Ref.1

Sequence conflict

122

1

L → R in AAP41950. Ref.1

Sequence conflict

799

1

R → C in AAP41950. Ref.1

Sequence conflict

867

1

R → C in AAP41950. Ref.1

Sequence conflict

895

1

Y → Q in AAP41950. Ref.1

Sequence conflict

1007

1

S → F in AAP41950. Ref.1

Sequence conflict

1245

1

A → V in CAB86200. Ref.4

Sequence conflict

1421

1

S → D in AAA82929. Ref.5

Sequence conflict

1485 – 1486

2

IS → TL in AAA82929. Ref.5

Sequence conflict

2361

1

D → A in AAP41950. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2813

Helix Strand Turn

Details...

Beta strand

1274 – 1283

10

Beta strand

1285 – 1288

4

Helix

1290 – 1304

15

Beta strand

1311 – 1329

19

Helix

1337 – 1345

9

Helix

1357 – 1366

10

Turn

1367 – 1369

3

Beta strand

1377 – 1385

9

Helix

1391 – 1394

4

Helix

1397 – 1406

10

Beta strand

1409 – 1420

12

Helix

1422 – 1430

9

Beta strand

1438 – 1442

5

Helix

1443 – 1458

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 2. Checksum: 3EE2C7D8FF21FFA6	FASTA	2,813	309,269
	10 20 30 40 50 60 MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM YSFAGGCSYL 70 80 90 100 110 120 LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG TVMQGDQSIS MPYASQGLYL 130 140 150 160 170 180 ELEAGYYKLS SETFGFAARI DGNGNFQVLM SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL 190 200 210 220 230 240 TSDPYDFANS WALSSEEQRC KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL 250 260 270 280 290 300 VDPESFVALC EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME 310 320 330 340 350 360 YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC VHAGKRYPPG 370 380 390 400 410 420 TSLSQDCNTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCED 430 440 450 460 470 480 HTFSIVIETM QCADDPDAVC TRSVSVRLSA LHNSLVKLKH GGAVGIDGQD VQLPFLQGDL 490 500 510 520 530 540 RIQHTVMASV RLSYAEDLQM DWDGRGRLLV KLSPVYSGKT CGLCGNYNGN KGDDFLTPAG 550 560 570 580 590 600 LVEPLVVDFG NAWKLQGDCS DLRRQHSDPC SLNPRLTRFA EEACALLTSS KFEACHHAVS 610 620 630 640 650 660 PLPYLQNCRY DVCSCSDSRD CLCNAVANYA AECARKGVHI GWREPGFCAL GCPQGQVYLQ 670 680 690 700 710 720 CGNSCNLTCR SLSLPDEECS EVCLEGCYCP PGLYQDERGD CVPKAQCPCY YDGELFQPAD 730 740 750 760 770 780 IFSDHHTMCY CEDGFMHCTT SGTLGSLLPD TVLSSPLSHR SKRSLSCRPP MVKLVCPADN 790 800 810 820 830 840 PRAQGLECAK TCQNYDLERM SLGCVSGCLC PPGMVRHENK CVALERCPCF HQGAEYAPGD 850 860 870 880 890 900 TVKIGCNTCV CRERKWNCTN HVCDATRSAI GMAHYLTFDG LKYLFPGECQ YVLVYDYCGS 910 920 930 940 950 960 NPGTFQILVG NEGCSYPSVK CRKRVTILVD GGELELFDGE VNVKRPLRDE SHFEVVESGR 970 980 990 1000 1010 1020 YVILLLGQAL SVVWDHHLSI SVVLKHTYQE QVCGLCGNFD GIQNNDSTTS SLQVEEDPVN 1030 1040 1050 1060 1070 1080 FGNSWKVSSQ CADTRKLSLD VSPATCHNNI MKQTMVDSAC RILTSDVFQG CNRLVDPEPY 1090 1100 1110 1120 1130 1140 LDICIYDTCS CESIGDCACF CDTIAAYAHV CAQHGQVVAW RTPTLCPQSC EEKNVRENGY 1150 1160 1170 1180 1190 1200 ECEWRYNSCA PACPVTCQHP EPLACPVQCV EGCHAHCPPG RILDELLQTC VDPQDCPVCE 1210 1220 1230 1240 1250 1260 VAGRRLAPGK KITLSPDDPA HCQNCHCDGV NLTCEACQEP GGLVAPPTDA PVSSTTPYVE 1270 1280 1290 1300 1310 1320 DTPEPPLHNF YCSKLLDLVF LLDGSSMLSE AEFEVLKAFV VGMMERLHIS QKRIRVAVVE 1330 1340 1350 1360 1370 1380 YHDGSRAYLE LKARKRPSEL RRITSQIKYT GSQVASTSEV LKYTLFQIFG KIDRPEASHI 1390 1400 1410 1420 1430 1440 TLLLTASQEP PRMARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIRLIEK QAPENKAFLL 1450 1460 1470 1480 1490 1500 SGVDELEQRR DEIVSYLCDL APEAPAPTQP PQVAHVTVSP GIAGISSPGP KRKSMVLDVV 1510 1520 1530 1540 1550 1560 FVLEGSDEVG EANFNKSKEF VEEVIQRMDV SPDATRISVL QYSYTVTMEY AFNGAQSKEE 1570 1580 1590 1600 1610 1620 VLRHVREIRY QGGNRTNTGQ ALQYLSEHSF SPSQGDRVEA PNLVYMVTGN PASDEIKRLP 1630 1640 1650 1660 1670 1680 GDIQVVPIGV GPHANMQELE RISRPIAPIF IRDFETLPRE APDLVLQTCC SKEGLQLPTL 1690 1700 1710 1720 1730 1740 PPLPDCSQPL DVVLLLDGSS SLPESSFDKM KSFAKAFISK ANIGPHLTQV SVIQYGSINT 1750 1760 1770 1780 1790 1800 IDVPWNVVQE KAHLQSLVDL MQQEGGPSQI GDALAFAVRY VTSQIHGARP GASKAVVIII 1810 1820 1830 1840 1850 1860 MDTSLDPVDT AADAARSNRV AVFPVGVGDR YDEAQLRILA GPGASSNVVK LQQVEDLSTM 1870 1880 1890 1900 1910 1920 ATLGNSFFHK LCSGFSGVCV DEDGNEKRPG DVWTLPDQCH TVTCLANGQT LLQSHRVNCD 1930 1940 1950 1960 1970 1980 HGPRPSCANS QSPVRVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVIFQNK 1990 2000 2010 2020 2030 2040 EQDLEVLLHN GACSPGAKQA CMKSIEIKHA GVSAELHSNM EMAVDGRLVL APYVGENMEV 2050 2060 2070 2080 2090 2100 SIYGAIMYEV RFTHLGHILT YTPQNNEFQL QLSPKTFASK MHGLCGICDE NGANDFTLRD 2110 2120 2130 2140 2150 2160 GTVTTDWKRL VQEWTVQQPG YTCQAVPEEQ CPVSDSSHCQ VLLSASFAEC HKVIAPATFH 2170 2180 2190 2200 2210 2220 TICQQDSCHQ ERVCEVIASY AHLCRTSGVC VDWRTTDFCA MSCPPSLVYN HCERGCPRHC 2230 2240 2250 2260 2270 2280 DGNTSFCGDH PSEGCFCPQH QVFLEGSCVP EEACTQCVGE DGVRHQFLET WVPDHQPCQI 2290 2300 2310 2320 2330 2340 CMCLSGRKIN CTAQPCPTAR APTCGPCEVA RLKQSTNLCC PEYECVCDLF NCNLPPVPPC 2350 2360 2370 2380 2390 2400 EGGLQPTLTN PGECRPTFTC DCRKEECKRV SPPSCPPHRT PTLRKTQCCD EYECACSCVN 2410 2420 2430 2440 2450 2460 STLSCPLGYL ASATTNDCGC TTTTCLPDKV CVHRGTVYPV GQFWEEGCDT CTCTDMEDTV 2470 2480 2490 2500 2510 2520 VGLRVVQCSQ RPCEDSCQPG FSYVLHEGEC CGRCLPSACK VVAGSLRGDS HSSWKSVGSR 2530 2540 2550 2560 2570 2580 WAVPENPCLV NECVRVEDAV FVQQRNISCP QLAVPTCPTG FQLNCETSEC CPSCHCEPVE 2590 2600 2610 2620 2630 2640 ACLLNGTIIG PGKSVMVDLC TTCRCIVQTD AISRFKLECR KTTCEACPMG YREEKSQGEC 2650 2660 2670 2680 2690 2700 CGRCLPTACT IQLRGGRIMT LKQDETFQDG CDSHLCRVNE RGEYIWEKRV TGCPPFDEHK 2710 2720 2730 2740 2750 2760 CLAEGGKIVK IPGTCCDTCE EPDCKDITAK VQYIKVGDCK SQEEVDIHYC QGKCASKAVY 2770 2780 2790 2800 2810 SIDIEDVQEQ CSCCLPSRTE PMRVPLHCTN GSVVYHEVIN AMQCRCSPRN CSK
	Isoform 2. Checksum: 36201FC93F1EE915	FASTA	402	44,467
	10 20 30 40 50 60 MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM YSFAGGCSYL 70 80 90 100 110 120 LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG TVMQGDQSIS MPYASQGLYL 130 140 150 160 170 180 ELEAGYYKLS SETFGFAARI DGNGNFQVLM SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL 190 200 210 220 230 240 TSDPYDFANS WALSSEEQRC KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL 250 260 270 280 290 300 VDPESFVALC EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME 310 320 330 340 350 360 YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC VHAGKRYPPG 370 380 390 400 TSLSQDCNTC ICRNSLWICS NEECPGRLGT FSPFLPVLCG EV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of full-length murine von Willebrand factor cDNA." Chitta M.S., Duhe R.J., Kermode J.C. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Lung.
[2]	"Murine von Willebrand factor." Lenting P.J., Westein E., de Groot P.G., Denis C.V. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Hippocampus.
[4]	"Variance of molecular datings, evolution of rodents and the phylogenetic affinities between Ctenodactylidae and Hystricognathi." Huchon D., Catzeflis F.M., Douzery E.J.P. Proc. R. Soc. B 267:393-402(2000) [PubMed: 10722222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1238-1658 (ISOFORM 1).
[5]	"von Willebrand disease in the RIIIS/J mouse is caused by a defect outside of the von Willebrand factor gene." Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E., Reddington M., Novak E.K., Swank R.T., Ginsburg D. Blood 83:3225-3231(1994) [PubMed: 8193357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1298-1684 (ISOFORM 1). Strain: BALB/c.
[6]	Erratum Nichols W.C., Cooney K.A., Mohlke K.L., Ballew J.D., Yang A., Bruck M.E., Reddington M., Novak E.K., Swank R.T., Ginsburg D. Blood 86:2461-2461(1995) [PubMed: 7662996] [Abstract]
[7]	"An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation." Lenting P.J., Westein E., Terraube V., Ribba A.-S., Huizinga E.G., Meyer D., de Groot P.G., Denis C.V. J. Biol. Chem. 279:12102-12109(2004) [PubMed: 14613933] [Abstract] Cited for: MUTAGENESIS OF ARG-1205, TISSUE SPECIFICITY. Strain: C57BL/6J.
[8]	"von Willebrand factor, platelets and endothelial cell interactions." Ruggeri Z.M. J. Thromb. Haemost. 1:1335-1342(2003) [PubMed: 12871266] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY208897 mRNA. Translation: AAP41950.1.
AY162409 mRNA. Translation: AAN73055.1.
AF539800 mRNA. Translation: AAN07781.2.
AK083237 mRNA. Translation: BAC38822.1. Different initiation.
AJ238390 Genomic DNA. Translation: CAB86200.1.
U27810 Genomic DNA. Translation: AAA82929.1.

IPI

IPI00798576.
IPI00830789.

RefSeq

NP_035838.3.

UniGene

Mm.22339

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U0O	X-ray	2.70	C	1261-1468	[»]

SMR

Q8CIZ8. Positions 293-361, 650-719, 1684-1873.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8CIZ8.

Protein family/group databases

MEROPS

I08.950.
I08.954.

PTM databases

PhosphoSite

Q8CIZ8.

Proteomic databases

PRIDE

Q8CIZ8.

Genome annotation databases

Ensembl

ENSMUST00000001995; ENSMUSP00000001995; ENSMUSG00000001930; Mus musculus. [Genome view]
ENSMUST00000112254; ENSMUSP00000107873; ENSMUSG00000001930; Mus musculus. [Genome view]
ENSMUST00000112262; ENSMUSP00000107881; ENSMUSG00000001930; Mus musculus. [Genome view]

GeneID

22371.

KEGG

mmu:22371.

Organism-specific databases

CTD

22371.

MGI

MGI:98941. Vwf.

Phylogenomic databases

HOGENOM

HBG444837.

HOVERGEN

Q8CIZ8.

InParanoid

Q8CIZ8.

Gene expression databases

ArrayExpress

Q8CIZ8.

Bgee

Q8CIZ8.

CleanEx

MM_VWF.

Genevestigator

Q8CIZ8.

GermOnline

ENSMUSG00000001930. Mus musculus.

Family and domain databases

InterPro

IPR014853. Conserved-cysteine-rich_domain.
IPR006207. Cys_knot_C.
IPR002919. Prot_Inh_CR_TIL.
IPR018453. Prot_Inh_CR_TIL_sg.
IPR001846. von_Willebrand_fac_D.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view]

PIRSF

PIRSF002495. VWF. 1 hit.

SMART

SM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]

PROSITE

PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS50234. VWFA. 3 hits.
PS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
PS51233. VWFD. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

302707.

SOURCE

Search...

Entry information

Entry name

VWF_MOUSE

Accession

Primary (citable) accession number: Q8CIZ8
Secondary accession number(s): Q60863 , Q6XUV6, Q8BIU9, Q8CGN0, Q9JK16

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	October 1, 2003
Last modified:	January 19, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)