Q28833 (VWF_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
von Willebrand factor
Short name=vWF

Gene names

Name:	VWF
Synonyms:	F8VWF

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	2482 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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, glycoprotein Ibalpha/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.
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.
Domain	The propeptide 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. N- and O-glycosylated By similarity.
Sequence similarities	Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 3 TIL (trypsin inhibitory-like) domains. Contains 3 VWFA domains. Contains 3 VWFC domains. Contains 3 VWFD domains.

Ontologies

Keywords
Biological process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Extracellular matrix Secreted
Domain	Repeat
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-substrate adhesion Inferred from sequence or structural similarity. Source: UniProtKB 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 extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB extracellular region Inferred from sequence or structural similarity. Source: UniProtKB 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	‹1 – 437	›437	By similarity		PRO_0000022686
	Chain	438 – 2482	2045	von Willebrand factor		PRO_0000022687
Regions
	Domain	61 – 272	212	VWFD 1
	Domain	326 – 381	56	TIL 1
	Domain	450 – 501	52	TIL 2
	Domain	540 – 748	209	VWFD 2
	Domain	820 – 870	51	TIL 3
	Domain	947 – 1127	181	VWFA 1
	Domain	1167 – 1334	168	VWFA 2
	Domain	1360 – 1540	181	VWFA 3
	Domain	1618 – 1822	205	VWFD 3
	Domain	1924 – 1997	74	VWFC 1
	Domain	2098 – 2164	67	VWFC 2
	Domain	2249 – 2314	66	VWFC 3
	Domain	2393 – 2481	89	CTCK
	Region	438 – 461	24	Amino-terminal
	Region	462 – 507	46	E1
	Region	500 – 527	28	CX
	Region	1885 – 1930	46	E2
	Motif	2176 – 2178	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	905	1	N-linked (GlcNAc...) Potential
	Glycosylation	1184	1	N-linked (GlcNAc...) Potential
	Glycosylation	1243	1	N-linked (GlcNAc...) Potential
	Glycosylation	1640	1	N-linked (GlcNAc...) Potential
	Glycosylation	1892	1	N-linked (GlcNAc...) Potential
	Glycosylation	1959	1	N-linked (GlcNAc...) Potential
	Glycosylation	2026	1	N-linked (GlcNAc...) Potential
	Glycosylation	2069	1	N-linked (GlcNAc...) Potential
	Glycosylation	2215	1	N-linked (GlcNAc...) Potential
	Glycosylation	2254	1	N-linked (GlcNAc...) Potential
	Glycosylation	2459	1	N-linked (GlcNAc...) Potential
	Disulfide bond	441 ↔ 482		By similarity
	Disulfide bond	450 ↔ 478		By similarity
	Disulfide bond	484 ↔ 495		By similarity
	Disulfide bond	541 ↔ 670		By similarity
	Disulfide bond	563 ↔ 705		By similarity
	Disulfide bond	572 ↔ 667		By similarity
	Disulfide bond	588 ↔ 595		By similarity
	Disulfide bond	734 ↔ 758		By similarity
	Disulfide bond	745 ↔ 785		By similarity
	Disulfide bond	763 ↔ 765		By similarity
	Disulfide bond	800 ↔ 804		By similarity
	Disulfide bond	823 ↔ 843		By similarity
	Disulfide bond	827 ↔ 839		By similarity
	Disulfide bond	870 ↔ 873		By similarity
	Disulfide bond	908 ↔ 911		By similarity
	Disulfide bond	942 ↔ 1128		By similarity
	Disulfide bond	1338 ↔ 1339		By similarity
	Disulfide bond	1355 ↔ 1541		By similarity
	Disulfide bond	1548 ↔ 1573		By similarity
	Disulfide bond	1568 ↔ 1609		Or C-1568 with C-1611 By similarity
	Disulfide bond	1596 ↔ 1757		By similarity
	Disulfide bond	1619 ↔ 1754		By similarity
	Disulfide bond	1641 ↔ 1792		By similarity
	Disulfide bond	1662 ↔ 1670		By similarity
	Disulfide bond	2393 ↔ 2443		By similarity
	Disulfide bond	2408 ↔ 2457		By similarity
	Disulfide bond	2419 ↔ 2473		By similarity
	Disulfide bond	2423 ↔ 2475		By similarity
	Disulfide bond	? ↔ 2480		By similarity
	Cross-link	1389		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q28833 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: D499B7DDFBBCAEDD	FASTA	2,482	272,397
	10 20 30 40 50 60 DGCSCPEGQL LDDGRCVESA ECSCVHSGKR YPPGASLSRD CNTCICRNSL WVCSNEDCPG 70 80 90 100 110 120 ECLVTGQSHF KSFDNRHFTF SGVCQYLLAR DCQDHTFSVI IETVQCADDP DAVCTRSVTV 130 140 150 160 170 180 RLPSPHNSLV KLKHGGGVAM DGWDVQIPFL QGDLRIQHTV MASVHLSYGE DLQIDWDGRG 190 200 210 220 230 240 RLLVKLSPVY AGRTCGLCGN YNGNQGDDFL TPAGLVEPLV EHFGNAWKLH GDCEDLRKQP 250 260 270 280 290 300 TDPCSFNPRL TRFAEEACAI LTSPKFQACH DAVGPLPYLQ NCHYDVCSCS DGRDCLCDAV 310 320 330 340 350 360 ATYAAACARR GVHIGWREPG FCALSCPPGQ VYLQCGTPCN LTCRSLSYPD EECAEDCLEG 370 380 390 400 410 420 CFCPPGLYLD GSGDCVPKAQ CPCYHDGEIF QPEDIFSDHH TMCYCEDGFM HCSRAGAPGS 430 440 450 460 470 480 LQPEVVLSSP LSHRSKRSLS CRPPMVKLVC PADNPRAEGL ECAKTCQNYD LECVSTGCVS 490 500 510 520 530 540 GCLCPPGMVR HENRCVALQR CPCFHQGREY APGETVKVDC NTCVCRDRKW SCTDHVCDAS 550 560 570 580 590 600 CSALGLAHYL TFDGLKYLFP GECQYVLVQD YCGSNPGTFR ILLGNEGCGY PSLKCRKRVT 610 620 630 640 650 660 ILVDGGEIEL FDGEVMVKKP LKDETHFEVV ESGRFITVLL GSGLSVVWDR HLGISVFLKQ 670 680 690 700 710 720 TYQEQVCGLC GNFDGVQNND LTGSSLQVEE DPVDFGNSWK VSPQCADTRK VPLDTSPATC 730 740 750 760 770 780 HNNVMKQTMV DSSCRILTSD IFQDCNKLVD PEPYLDVCIY DTCSCESIGD CACFCDTIAA 790 800 810 820 830 840 YARVCAQHGK VVTWRTATLC PQNCEERNLR EDGYQCEWRY NSCAPACPVT CQHPEPLACP 850 860 870 880 890 900 VSCVEGCHAH CPPGKILDEL LQTCVSPEDC PVCEAAGRRL APGKKIILNP RDPAHCQICH 910 920 930 940 950 960 CDGVNLTCEA CAEPVPPTEG PVSPTTPYEE DTPEPPLHDF FCSKLLDLVF LLDGSDKLSE 970 980 990 1000 1010 1020 ADFEALKVFV VGMMEHLHIS QKHIRVAVVE YHDGPHAYIS LQDRKRPSEL RRIASQVKYA 1030 1040 1050 1060 1070 1080 GSEVASISEV LKYTLFQIFG RVDRPEASRI ALLLMASQEP RRLAQNLARY LQGLKKKKVT 1090 1100 1110 1120 1130 1140 VIPVGIGPHV SLKQIRLIEK QAPENKAFVV SGVDELEQRK NEIISYLCDL APEVPAPTRR 1150 1160 1170 1180 1190 1200 PLVAQVTVAP ELPGVSTLEP KKRMALDVVF VLEGSDKVGE ANFNRSTEFV EEVIRRMDVG 1210 1220 1230 1240 1250 1260 RDSVHVTVLQ YSYVVAVEHS FREAQSKGEV LQRVREIRFQ GGNRTNTGLA LQYLSEHSFS 1270 1280 1290 1300 1310 1320 ASQGDREEAP NLVYMVTGNP ASDEIKRMPG DIQVVPIGVG PDVDMQELER LSWPNAPIFI 1330 1340 1350 1360 1370 1380 QDFETLPREA PDLVLQRCCS GEGPHLPTQA PVPDCSQPLG VVLLLDGSSS LPASYFDEMK 1390 1400 1410 1420 1430 1440 SFTKAFISKA NIGPQLTQVS VLQYGSITTI DLPWNMPLEK AHLRGLVDLM QREGGPSQIG 1450 1460 1470 1480 1490 1500 DALGFAVRYV MSQVHGARPE ASKAVVIVVT DTSTDSVDAA AAAARSNRVA VFPIGIGDRY 1510 1520 1530 1540 1550 1560 DEAQLRTLAG PGASSNVVKL QRIEDLPTLV TLGNSFLHKL CSGFVRVCID EDGSERKPGD 1570 1580 1590 1600 1610 1620 VWTLPDQCHT VTCLPDGQTL LKSHRVNCDQ GLQPSCPSNQ PPIRVEEACG CRWTCPCVCT 1630 1640 1650 1660 1670 1680 GSSTRHIVTF DGQNFKLMGN CSYVLFHNKE QDLEVILHNG ACGAGARQAC MKSIEVKHNG 1690 1700 1710 1720 1730 1740 LSVELHRDME VVVNGRQVSV PYVGGNMEVG IYGTIMYEVR FNHLGHILTF TPQNNEFQLQ 1750 1760 1770 1780 1790 1800 LSPKTFASKM YGLCGICDEN GANDFMLRDG TVTTDWKTMV QEWAVQQPGQ MCQPVPKEQC 1810 1820 1830 1840 1850 1860 PVSGGYQCQV LLSALFAECH KVLAPAAYFA ICQQDSCHQE QVCEAVASYA HLCRTKGVCV 1870 1880 1890 1900 1910 1920 DWRTPDFCAV SCPPSLVYNH CEHGCPRHCE GNSSSCGDHP SEGCFCPPHQ VMLGSSCVPE 1930 1940 1950 1960 1970 1980 EACTQCVDDD GIRHQFLETW VPDHQPCQIC TCLSGRRVNC TLQPCPTARA PACGLCEVAR 1990 2000 2010 2020 2030 2040 LRQEAHQCCP EYECVCDLVS CDLPPVPHCE GGLQPTLTNP GECRPNFTCA CRKEECPRGP 2050 2060 2070 2080 2090 2100 LPSCPPHRTP ALRKTQCCDE YECACNCVNT TLSCPLGYLA STVTNDCGCT TTTCLPDKVC 2110 2120 2130 2140 2150 2160 VHRGTVYPVG QFWEEGCDVC TCTDLEDAVM GLRVAQCAQK PCEDSCRPGF TYVLHEGECC 2170 2180 2190 2200 2210 2220 GKCLPSACKV VIGSFRGDSV SYWKSVGSHW ASPENPCLIN ECVRVKEEVF VQQRNVSCPM 2230 2240 2250 2260 2270 2280 LDVPTCPVGF QLSCKTSGCC PTCRCEPVEA CLLNGTIIGA GESLMIDVCT TCRCMLQEGV 2290 2300 2310 2320 2330 2340 VFGFKLECKK TTCEACPLGY KEEKMPGECC GRCLPTACTI QLRGGQIMTL KRDETLQDGC 2350 2360 2370 2380 2390 2400 DSHFCRVNER GEYIWEKRIT GCPPFDQHKC LAAGGKIMKI PGTCCDTCEE PECKDMTARL 2410 2420 2430 2440 2450 2460 QYVKVGNCRS EEEVDIHYCQ GKCTSKAVYS IDTEDVEDQC ACCSPTRTEP MQVPLRCTNG 2470 2480 STIYHEVLNA IQCKCSPRKC SK

References

[1]	Seaman W.T., Read M.S., Bellinger D.A., Nichols T.C. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Primary structure of the factor VIII binding domain of human, porcine and rabbit von Willebrand factor." Lavergne J.-M., Piao Y.C., Ferreira V., Kerbiriou-Nabias D., Bahnak B.R., Meyer D. Biochem. Biophys. Res. Commun. 194:1019-1024(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 397-553.
[3]	"von Willebrand factor, platelets and endothelial cell interactions." Ruggeri Z.M. J. Thromb. Haemost. 1:1335-1342(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF052036 mRNA. Translation: AAC06229.1. S64541 mRNA. Translation: AAB27829.2.
PIR	PN0563.
UniGene	Ssc.978.
3D structure databases
ProteinModelPortal	Q28833.
SMR	Q28833. Positions 931-1138, 1353-1542.
ModBase	Search...
Proteomic databases
PaxDb	Q28833.
PRIDE	Q28833.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG004380.
Family and domain databases
InterPro	IPR006207. Cys_knot_C. IPR000742. EG-like_dom. IPR002919. TIL_dom. IPR014853. Unchr_dom_Cys-rich. IPR002035. VWF_A. IPR001007. VWF_C. IPR001846. VWF_type-D. [Graphical view]
Pfam	PF08742. C8. 3 hits. PF01826. TIL. 4 hits. PF00092. VWA. 3 hits. PF00093. VWC. 2 hits. PF00094. VWD. 3 hits. [Graphical view]
SMART	SM00832. C8. 3 hits. SM00041. CT. 1 hit. SM00181. EGF. 1 hit. SM00327. VWA. 3 hits. SM00214. VWC. 5 hits. SM00216. VWD. 3 hits. [Graphical view]
SUPFAM	SSF57567. Cysrich_TIL. 4 hits.
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. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VWF_PIG

Accession

Primary (citable) accession number: Q28833

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program