VWC2L_MOUSE
ID VWC2L_MOUSE Reviewed; 222 AA.
AC Q505H4; B7X8X0; E0CXU0; E6Y2G9; Q8BNE9; Q8BNU5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=von Willebrand factor C domain-containing protein 2-like;
DE AltName: Full=Brorin-like;
DE Flags: Precursor;
GN Name=Vwc2l;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19852960; DOI=10.1016/j.febslet.2009.10.044;
RA Miwa H., Miyake A., Kouta Y., Shimada A., Yamashita Y., Nakayama Y.,
RA Yamauchi H., Konishi M., Itoh N.;
RT "A novel neural-specific BMP antagonist, Brorin-like, of the Chordin
RT family.";
RL FEBS Lett. 583:3643-3648(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=22209847; DOI=10.1016/j.bbrc.2011.12.075;
RA Ohyama Y., Katafuchi M., Almehmadi A., Venkitapathi S., Jaha H.,
RA Ehrenman J., Morcos J., Aljamaan R., Mochida Y.;
RT "Modulation of matrix mineralization by Vwc2-like protein and its novel
RT splicing isoforms.";
RL Biochem. Biophys. Res. Commun. 418:12-16(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal ganglion;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
CC -!- FUNCTION: May play a role in neurogenesis. May promote matrix
CC mineralization (PubMed:22209847), but has been shown to weakly, but
CC significantly inhibit BMP2 and BMP6 activity in a preosteoblastic cell
CC line (PubMed:19852960). {ECO:0000269|PubMed:19852960,
CC ECO:0000269|PubMed:22209847}.
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including VWC2L. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing. {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Secreted. Synapse {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=F12-a, Vwc2l-1;
CC IsoId=Q505H4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q505H4-2; Sequence=VSP_035091;
CC Name=3;
CC IsoId=Q505H4-3; Sequence=VSP_035090, VSP_035092, VSP_035093;
CC Name=4; Synonyms=F12-b, Vwc2l-2;
CC IsoId=Q505H4-4; Sequence=VSP_044591, VSP_044592;
CC Name=5; Synonyms=F12-c, Vwc2l-3;
CC IsoId=Q505H4-5; Sequence=VSP_035091, VSP_044591, VSP_044592;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein
CC level). Also detected in bones, including femur and calvaria, heart,
CC lung and kidney. Isoform 5 is predominant in lung and heart, compared
CC to isoforms 1 and 3. Isoform 4 is expressed in femur and calvaria at
CC higher levels than isoforms 1 and 5. Isoforms 1 and 4 are expressed at
CC higher levels than isoform 5 in kidney and brain.
CC {ECO:0000269|PubMed:19852960, ECO:0000269|PubMed:22209847,
CC ECO:0000269|PubMed:22632720}.
CC -!- DEVELOPMENTAL STAGE: From 12.5 dpc to 18.5 dpc, expressed in the
CC developing neural tissues, including several discrete regions in the
CC forebrain, midbrain and hindbrain, as well as in the spinal cord. May
CC be up-regulated in the course of preosteblast differentiation and
CC matrix mineralization. {ECO:0000269|PubMed:19852960,
CC ECO:0000269|PubMed:22209847}.
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DR EMBL; AB374230; BAH04175.1; -; mRNA.
DR EMBL; EF552208; ABU41138.1; -; mRNA.
DR EMBL; EF552209; ABU41139.1; -; mRNA.
DR EMBL; EF552210; ABU41140.1; -; mRNA.
DR EMBL; AK080585; BAC37948.1; -; mRNA.
DR EMBL; AK083856; BAC39040.1; -; mRNA.
DR EMBL; AC129933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094541; AAH94541.1; -; mRNA.
DR CCDS; CCDS15028.1; -. [Q505H4-1]
DR CCDS; CCDS78606.1; -. [Q505H4-4]
DR RefSeq; NP_001297587.1; NM_001310658.1. [Q505H4-4]
DR RefSeq; NP_796138.2; NM_177164.3. [Q505H4-1]
DR RefSeq; XP_006496126.1; XM_006496063.3. [Q505H4-1]
DR AlphaFoldDB; Q505H4; -.
DR SMR; Q505H4; -.
DR STRING; 10090.ENSMUSP00000058142; -.
DR PhosphoSitePlus; Q505H4; -.
DR PaxDb; Q505H4; -.
DR PRIDE; Q505H4; -.
DR ProteomicsDB; 299735; -. [Q505H4-1]
DR ProteomicsDB; 299736; -. [Q505H4-2]
DR ProteomicsDB; 299737; -. [Q505H4-3]
DR ProteomicsDB; 299738; -. [Q505H4-4]
DR Antibodypedia; 52490; 12 antibodies from 6 providers.
DR DNASU; 320460; -.
DR Ensembl; ENSMUST00000053922; ENSMUSP00000058142; ENSMUSG00000045648. [Q505H4-1]
DR Ensembl; ENSMUST00000161937; ENSMUSP00000125014; ENSMUSG00000045648. [Q505H4-4]
DR Ensembl; ENSMUST00000162182; ENSMUSP00000123819; ENSMUSG00000045648. [Q505H4-2]
DR GeneID; 320460; -.
DR KEGG; mmu:320460; -.
DR UCSC; uc007bjj.1; mouse. [Q505H4-4]
DR UCSC; uc007bjk.1; mouse. [Q505H4-1]
DR UCSC; uc011wmo.1; mouse. [Q505H4-2]
DR UCSC; uc011wmp.1; mouse. [Q505H4-5]
DR CTD; 402117; -.
DR MGI; MGI:2444069; Vwc2l.
DR VEuPathDB; HostDB:ENSMUSG00000045648; -.
DR eggNOG; ENOG502RAAU; Eukaryota.
DR GeneTree; ENSGT00720000108792; -.
DR HOGENOM; CLU_100254_2_0_1; -.
DR InParanoid; Q505H4; -.
DR OMA; PICKHGP; -.
DR OrthoDB; 1478107at2759; -.
DR PhylomeDB; Q505H4; -.
DR TreeFam; TF329913; -.
DR BioGRID-ORCS; 320460; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Vwc2l; mouse.
DR PRO; PR:Q505H4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q505H4; protein.
DR Bgee; ENSMUSG00000045648; Expressed in substantia nigra and 40 other tissues.
DR Genevisible; Q505H4; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR InterPro; IPR042979; VWC2/VWC2L.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46252; PTHR46252; 1.
DR SMART; SM00214; VWC; 2.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Reference proteome; Repeat;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..222
FT /note="von Willebrand factor C domain-containing protein 2-
FT like"
FT /id="PRO_0000348062"
FT DOMAIN 51..110
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 114..172
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT VAR_SEQ 1..35
FT /note="MALHIHEACILLLVIPGLVTSAAISHEDYPADEGD -> MKLAYFYWSSLDW
FT SPLLPSVTKTILLMKVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035090"
FT VAR_SEQ 34..80
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:22209847"
FT /id="VSP_035091"
FT VAR_SEQ 131..139
FT /note="PSPCEWCRC -> VQTALQELQ (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:22209847"
FT /id="VSP_044591"
FT VAR_SEQ 131
FT /note="P -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035092"
FT VAR_SEQ 132..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035093"
FT VAR_SEQ 140..222
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:22209847"
FT /id="VSP_044592"
SQ SEQUENCE 222 AA; 24528 MW; 6F40D6393609DD54 CRC64;
MALHIHEACI LLLVIPGLVT SAAISHEDYP ADEGDQASSN DNLIFDDYRG KGCVDDSGFV
YKLGERFFPG HSNCPCVCAL DGPVCDQPEC PKIHPKCTKV EHNGCCPECK EVKNFCEYHG
KNYKILEEFK PSPCEWCRCE PSNEVHCVVA DCAVPECVNP IYEPEQCCPV CKNGPNCFAG
TTIIPAGIEV KVDDCNICHC HNGDWWKPAQ CSKRECQGKQ TV
