VWA1_MOUSE
ID VWA1_MOUSE Reviewed; 415 AA.
AC Q8R2Z5; Q8C0Q7; Q8VDV9; Q923K3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=von Willebrand factor A domain-containing protein 1;
DE AltName: Full=von Willebrand factor A domain-related protein;
DE Flags: Precursor;
GN Name=Vwa1; Synonyms=Warp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, GLYCOSYLATION, DISULFIDE
RP BOND, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12062410; DOI=10.1016/s0014-5793(02)02579-6;
RA Fitzgerald J., Tay Ting S., Bateman J.F.;
RT "WARP is a new member of the von Willebrand factor A-domain superfamily of
RT extracellular matrix proteins.";
RL FEBS Lett. 517:61-66(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Ovary, Testis, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH HSPG2,
RP AND MUTAGENESIS OF CYS-369 AND CYS-393.
RX PubMed=16407285; DOI=10.1074/jbc.m513746200;
RA Allen J.M., Bateman J.F., Hansen U., Wilson R., Bruckner P., Owens R.T.,
RA Sasaki T., Timpl R., Fitzgerald J.;
RT "WARP is a novel multimeric component of the chondrocyte pericellular
RT matrix that interacts with perlecan.";
RL J. Biol. Chem. 281:7341-7349(2006).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18314316; DOI=10.1016/j.matbio.2008.01.005;
RA Allen J.M., Brachvogel B., Farlie P.G., Fitzgerald J., Bateman J.F.;
RT "The extracellular matrix protein WARP is a novel component of a distinct
RT subset of basement membranes.";
RL Matrix Biol. 27:295-305(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- FUNCTION: Promotes matrix assembly (PubMed:18757743). Involved in the
CC organization of skeletal muscles and in the formation of neuromuscular
CC junctions (By similarity). {ECO:0000250|UniProtKB:E7FF10,
CC ECO:0000269|PubMed:18757743}.
CC -!- SUBUNIT: Homodimer or homomultimer; disulfide-linked. Interacts with
CC HSPG2. {ECO:0000269|PubMed:12062410, ECO:0000269|PubMed:16407285}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:12062410,
CC ECO:0000269|PubMed:16407285, ECO:0000269|PubMed:18757743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2Z5-2; Sequence=VSP_028618;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the chondrocytes.
CC Detected in the vasculature of neural tissues, in basement membrane
CC structures of the peripheral nervous system, in the apical ectodermal
CC ridge of developing limb buds, and in skeletal and cardiac muscle (at
CC protein level). {ECO:0000269|PubMed:12062410,
CC ECO:0000269|PubMed:18314316}.
CC -!- DEVELOPMENTAL STAGE: Restricted to the presumptive articular cartilage
CC zone prior to joint cavitation and to the articular cartilage and
CC fibrocartilaginous elements in the joint, spine and sternum during
CC embryonic development. Detected from 9.5 dpc in the vasculature of the
CC central nervous system. At 16.5 dpc, present in intervertebral disks of
CC the spinal cord, lip epithelium and developing oral and tooth germ
CC epithelia (at protein level). {ECO:0000269|PubMed:16407285,
CC ECO:0000269|PubMed:18314316, ECO:0000269|PubMed:18757743}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12062410}.
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DR EMBL; AY030094; AAK38350.1; -; mRNA.
DR EMBL; AK030019; BAC26739.1; -; mRNA.
DR EMBL; AK077240; BAC36703.1; -; mRNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020136; AAH20136.1; -; mRNA.
DR EMBL; BC026919; AAH26919.1; -; mRNA.
DR EMBL; BC036166; AAH36166.1; -; mRNA.
DR CCDS; CCDS19039.1; -. [Q8R2Z5-1]
DR RefSeq; NP_680085.3; NM_147776.4. [Q8R2Z5-1]
DR RefSeq; XP_011248558.1; XM_011250256.1. [Q8R2Z5-2]
DR AlphaFoldDB; Q8R2Z5; -.
DR SMR; Q8R2Z5; -.
DR STRING; 10090.ENSMUSP00000040405; -.
DR GlyGen; Q8R2Z5; 1 site.
DR PhosphoSitePlus; Q8R2Z5; -.
DR MaxQB; Q8R2Z5; -.
DR PaxDb; Q8R2Z5; -.
DR PeptideAtlas; Q8R2Z5; -.
DR PRIDE; Q8R2Z5; -.
DR ProteomicsDB; 275194; -. [Q8R2Z5-1]
DR ProteomicsDB; 275195; -. [Q8R2Z5-2]
DR Antibodypedia; 26362; 73 antibodies from 22 providers.
DR DNASU; 246228; -.
DR Ensembl; ENSMUST00000042196; ENSMUSP00000040405; ENSMUSG00000042116. [Q8R2Z5-1]
DR GeneID; 246228; -.
DR KEGG; mmu:246228; -.
DR UCSC; uc008weq.2; mouse. [Q8R2Z5-1]
DR CTD; 64856; -.
DR MGI; MGI:2179729; Vwa1.
DR VEuPathDB; HostDB:ENSMUSG00000042116; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000160734; -.
DR HOGENOM; CLU_042926_0_0_1; -.
DR InParanoid; Q8R2Z5; -.
DR OMA; PEGVLNC; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; Q8R2Z5; -.
DR TreeFam; TF316402; -.
DR BioGRID-ORCS; 246228; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Vwa1; mouse.
DR PRO; PR:Q8R2Z5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R2Z5; protein.
DR Bgee; ENSMUSG00000042116; Expressed in sciatic nerve and 155 other tissues.
DR Genevisible; Q8R2Z5; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR030758; Vwa1.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020:SF51; PTHR24020:SF51; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..415
FT /note="von Willebrand factor A domain-containing protein 1"
FT /id="PRO_0000307157"
FT DOMAIN 34..209
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 214..305
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 307..403
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 391..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..393
FT /evidence="ECO:0000269|PubMed:12062410"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028618"
FT MUTAGEN 369
FT /note="C->S: No formation of homomultimers. No formation of
FT homodimers; when associated with S-393."
FT /evidence="ECO:0000269|PubMed:16407285"
FT MUTAGEN 393
FT /note="C->S: No formation of homomultimers. No formation of
FT homodimers; when associated with S-369."
FT /evidence="ECO:0000269|PubMed:16407285"
FT CONFLICT 98
FT /note="Q -> R (in Ref. 1; AAK38350)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="V -> A (in Ref. 2; BAC26739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 44709 MW; C3887963B2E334FE CRC64;
MLFWTAFSMA LSLRLALARS SIERGSTASD PQGDLLFLLD SSASVSHYEF SRVREFVGQL
VATMSFGPGA LRASLVHVGS QPHTEFTFDQ YSSGQAIQDA IRVAPQRMGD TNTGLALAYA
KEQLFAEEAG ARPGVPKVLV WVTDGGSSDP VGPPMQELKD LGVTIFIVST GRGNLLELLA
AASAPAEKHL HFVDVDDLPI IARELRGSIT DAMQPQQLHA SEVLSSGFRL SWPPLLTADS
GYYVLELVPS GKLATTRRQQ LPGNATSWTW TDLDPDTDYE VSLLPESNVH LLRPQHVRVR
TLQEEAGPER IVISHARPRS LRVSWAPALG PDSALGYHVQ LGPLQGGSLE RVEVPAGQNS
TTVQGLTPCT TYLVTVTAAF RSGRQRALSA KACTASGART RAPQSMRPEA GPREP
