ID   VWA1_BOVIN              Reviewed;         413 AA.
AC   A6QLN9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=von Willebrand factor A domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=VWA1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes matrix assembly (By similarity). Involved in the
CC       organization of skeletal muscles and in the formation of neuromuscular
CC       junctions (By similarity). {ECO:0000250|UniProtKB:E7FF10,
CC       ECO:0000250|UniProtKB:Q8R2Z5}.
CC   -!- SUBUNIT: Homodimer or homomultimer; disulfide-linked. Interacts with
CC       HSPG2. {ECO:0000250|UniProtKB:Q8R2Z5}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250|UniProtKB:Q8R2Z5}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8R2Z5}.
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DR   EMBL; BC148033; AAI48034.1; -; mRNA.
DR   RefSeq; NP_001096700.1; NM_001103230.1.
DR   AlphaFoldDB; A6QLN9; -.
DR   SMR; A6QLN9; -.
DR   STRING; 9913.ENSBTAP00000028372; -.
DR   PaxDb; A6QLN9; -.
DR   GeneID; 505917; -.
DR   KEGG; bta:505917; -.
DR   CTD; 64856; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3544; Eukaryota.
DR   HOGENOM; CLU_042926_0_0_1; -.
DR   InParanoid; A6QLN9; -.
DR   OrthoDB; 67372at2759; -.
DR   TreeFam; TF316402; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
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; IPR020592; Ribosomal_S16_CS.
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; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Basement membrane; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..413
FT                   /note="von Willebrand factor A domain-containing protein 1"
FT                   /id="PRO_0000307155"
FT   DOMAIN          32..211
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          212..302
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          305..395
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          385..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PCB0"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  43738 MW;  7103FD9328983CDC CRC64;
     MLPWTVIGLA LSLRLARSGA ERGLPASALQ GDLLFLLDSS ASVSHYEFNR VREFLGRLAA
     LLPVGPGALR ASLVHVGSRP HTEFPFGQHS SGSAVQDAIR AAAQRMGDTN TGLALAYAKK
     QLFAKAAGAR PGVPKVLVWV TDGGSSDPVG PPMQELKDLG VTVFIVSTGR GNLLELSAAA
     SAPAEKHLHF VDVDDLHIIT QALRGSILDA MWPQQLHASE VTSSGFRLAW PSLLTADSGY
     YVLELAPSTD PGAARRQQLP GNATGWAWTG LDSDTDYDVA LVPESNVRLL RSQHLRVRTL
     PEETGPELIV VSHTRPRSLR VSWAPALGPD AALGYHVQVG PLRGGAAQSV EVPAGENSTT
     LQGLAPGTAY LVTVTAAFRS GRERALSAKA CTPEGERSRA PRPQPQRTGG REP