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 27-MAR-2024, entry version 145.
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 GlyCosmos; Q70UZ7; 1 site, No reported glycans.
DR GlyGen; Q70UZ7; 1 site.
DR PhosphoSitePlus; Q70UZ7; -.
DR jPOST; Q70UZ7; -.
DR PaxDb; 10090-ENSMUSP00000026068; -.
DR ProteomicsDB; 297618; -. [Q70UZ7-1]
DR Antibodypedia; 46200; 112 antibodies from 22 providers.
DR DNASU; 240675; -.
DR Ensembl; ENSMUST00000026068.8; ENSMUSP00000026068.8; ENSMUSG00000025082.9. [Q70UZ7-1]
DR GeneID; 240675; -.
DR KEGG; mmu:240675; -.
DR UCSC; uc008hzl.1; mouse. [Q70UZ7-1]
DR AGR; MGI:2684334; -.
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; MWCSAAM; -.
DR OrthoDB; 5299728at2759; -.
DR PhylomeDB; Q70UZ7; -.
DR TreeFam; TF318242; -.
DR BioGRID-ORCS; 240675; 1 hit in 80 CRISPR screens.
DR PRO; PR:Q70UZ7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q70UZ7; Protein.
DR Bgee; ENSMUSG00000025082; Expressed in ear vesicle and 63 other cell types or tissues.
DR Genevisible; Q70UZ7; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
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 CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd01472; vWA_collagen; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24020:SF20; COLLAGEN ALPHA-1(XXI) CHAIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00092; VWA; 3.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF53300; vWA-like; 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
//
