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VWA2_MOUSE
ID   VWA2_MOUSE              Reviewed;         791 AA.
AC   Q70UZ7; Q14AY2; Q14BI0; Q3UM88;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=von Willebrand factor A domain-containing protein 2;
DE   AltName: Full=A domain-containing protein similar to matrilin and collagen;
DE            Short=AMACO;
DE   Flags: Precursor;
GN   Name=Vwa2; Synonyms=Amaco;
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), ALTERNATIVE SPLICING, DEVELOPMENTAL
RP   STAGE, TISSUE SPECIFICITY, AND SUBUNIT.
RC   STRAIN=C57BL/6J; TISSUE=Epiphyseal cartilage;
RX   PubMed=14506275; DOI=10.1074/jbc.m307794200;
RA   Sengle G., Kobbe B., Moergelin M., Paulsson M., Wagener R.;
RT   "Identification and characterization of AMACO, a new member of the von
RT   Willebrand factor A-like domain protein superfamily with a regulated
RT   expression in the kidney.";
RL   J. Biol. Chem. 278:50240-50249(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, Ovary, 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 MRNA] (ISOFORMS 1 AND 2).
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).
CC   -!- SUBUNIT: Forms monomers and multimers. {ECO:0000269|PubMed:14506275}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q70UZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q70UZ7-2; Sequence=VSP_028740, VSP_028741;
CC   -!- TISSUE SPECIFICITY: Detected in uterus, kidney, and skin. Also detected
CC       in intestine and lung of adult mice, and in calvaria, femur, brain,
CC       heart, intestine, skeletal muscle, and lung of newborn mice.
CC       {ECO:0000269|PubMed:14506275}.
CC   -!- DEVELOPMENTAL STAGE: First detected at days 7.5-8 dpc, when it is
CC       weakly expressed around the developing mesodermal cells. At day 10.5
CC       dpc it is detected in the heart and the condensing somites, and at day
CC       14.5 dpc it is present in the choroid plexus, the cochlea, the terminal
CC       bronchii of the lung, the heart, the skin, and in the cartilage
CC       primordium of the developing skeleton as well as in the interdigital
CC       spaces. Strong staining is seen in the condensed mesenchyme forming the
CC       edge of the developing teeth budding into the branchial arch and
CC       coinciding with the basement membrane that underlies the stratified
CC       squamous epithelia in the oral cavity. {ECO:0000269|PubMed:14506275}.
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DR   EMBL; AJ536329; CAD60277.1; -; mRNA.
DR   EMBL; AK133486; BAE21683.1; -; mRNA.
DR   EMBL; AK145058; BAE26210.1; -; mRNA.
DR   EMBL; BC115868; AAI15869.1; -; mRNA.
DR   EMBL; BC116636; AAI16637.1; -; mRNA.
DR   CCDS; CCDS29923.1; -. [Q70UZ7-1]
DR   RefSeq; NP_766428.2; NM_172840.2. [Q70UZ7-1]
DR   AlphaFoldDB; Q70UZ7; -.
DR   SMR; Q70UZ7; -.
DR   STRING; 10090.ENSMUSP00000026068; -.
DR   GlyGen; Q70UZ7; 1 site.
DR   PhosphoSitePlus; Q70UZ7; -.
DR   jPOST; Q70UZ7; -.
DR   PaxDb; Q70UZ7; -.
DR   PRIDE; Q70UZ7; -.
DR   ProteomicsDB; 297618; -. [Q70UZ7-1]
DR   Antibodypedia; 46200; 103 antibodies from 22 providers.
DR   DNASU; 240675; -.
DR   Ensembl; ENSMUST00000026068; ENSMUSP00000026068; ENSMUSG00000025082. [Q70UZ7-1]
DR   GeneID; 240675; -.
DR   KEGG; mmu:240675; -.
DR   UCSC; uc008hzl.1; mouse. [Q70UZ7-1]
DR   CTD; 340706; -.
DR   MGI; MGI:2684334; Vwa2.
DR   VEuPathDB; HostDB:ENSMUSG00000025082; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000159040; -.
DR   HOGENOM; CLU_008905_7_3_1; -.
DR   InParanoid; Q70UZ7; -.
DR   OMA; CWRGSRQ; -.
DR   PhylomeDB; Q70UZ7; -.
DR   TreeFam; TF318242; -.
DR   BioGRID-ORCS; 240675; 1 hit in 75 CRISPR screens.
DR   PRO; PR:Q70UZ7; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q70UZ7; protein.
DR   Bgee; ENSMUSG00000025082; Expressed in ear vesicle and 62 other tissues.
DR   Genevisible; Q70UZ7; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:MGI.
DR   Gene3D; 3.40.50.410; -; 3.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR030755; VWA2.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020:SF37; PTHR24020:SF37; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00092; VWA; 3.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00327; VWA; 3.
DR   SUPFAM; SSF53300; SSF53300; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50234; VWFA; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..791
FT                   /note="von Willebrand factor A domain-containing protein 2"
FT                   /id="PRO_5000070397"
FT   DOMAIN          51..221
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          295..332
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          342..516
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          530..704
FT                   /note="VWFA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          711..747
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          762..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        298..309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        303..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        321..331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        715..726
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        720..735
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        737..746
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         1..218
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028740"
FT   VAR_SEQ         219..268
FT                   /note="STLSSSALCTTADPDCRVEPHPCERRTLETVRELAGNALCWRGSRQADTV
FT                   -> MCCWLSKWRMPPMASSAPSAAPHSAPLLIQTAGWNLIPVSGGRWRPSGSS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028741"
FT   CONFLICT        18
FT                   /note="V -> A (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="V -> I (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="R -> Q (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="A -> E (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="G -> E (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="L -> V (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="V -> G (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511
FT                   /note="E -> K (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        713
FT                   /note="N -> D (in Ref. 2; BAE26210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        730
FT                   /note="N -> I (in Ref. 3; AAI16637)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   791 AA;  85639 MW;  863CEDEA32983790 CRC64;
     MPPLLLLPAI YMLLFFRVSP TISLQEVHVN RETMGKIAVA SKLMWCSAAV DILFLLDGSH
     SIGKGSFERS KRFAIAACDA LDISPGRVRV GALQFGSTPH LEFPLDSFST RQEVKESIKG
     IVFKGGRTET GLALKRLSRG FPGGRNGSVP QILIIVTDGK SQGPVALPAK QLRERGIVVF
     AVGVRFPRWD ELLTLASEPK DRHVLLAEQV EDATNGLLST LSSSALCTTA DPDCRVEPHP
     CERRTLETVR ELAGNALCWR GSRQADTVLA LPCPFYSWKR VFQTHPANCY RTICPGPCDS
     QPCQNGGTCI PEGVDRYHCL CPLAFGGEVN CAPKLSLECR IDVLFLLDSS AGTTLGGFRR
     AKAFVKRFVQ AVLREDSRAR VGIASYGRNL MVAVPVGEYQ HVPDLIRSLD SIPFSGGPTL
     TGSALLQVAE HGFGSASRTG QDRPRRVVVL LTESRSQDEV SGPAAHARAR ELLLLGVGSE
     ILQAELVKIT GSPKHVMVHT DPQDLFSQIP ELQRRLCSQP RPGCQAQSLD LVFLLDASAS
     VGRENFAQMQ SFIRKCTLRF DVNPDVTQVG LVVYGSRVQT AFGLDTHPTR AAVLRAMSQA
     PYLGGVGSAG TALLHIEDKV MTVQRGARPG VPKAVVMLTG GSGAEDAAVP AQKLRGNGIS
     VLVMSVGAVL REAVRRLAGP RDSLIHVAAY TDLPYHQDML IEWLCREARL PVNLCKPSPC
     MNEGTCVLKN GSYRCECRGG WEGPHCENRI LRGDAPMARS FHQEPAGLQG PTPSQQAPKH
     LRIGKALSSA K
 
 
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