VWC2_MOUSE
ID VWC2_MOUSE Reviewed; 324 AA.
AC Q8C8N3; B2RQ98; Q5SSH5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Brorin;
DE AltName: Full=Brain-specific chordin-like protein;
DE AltName: Full=CR (chordin-like cysteine-rich) domain-containing adhesive protein;
DE Short=Cradin;
DE AltName: Full=von Willebrand factor C domain-containing protein 2;
DE Flags: Precursor;
GN Name=Vwc2;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17400546; DOI=10.1074/jbc.m701570200;
RA Koike N., Kassai Y., Kouta Y., Miwa H., Konishi M., Itoh N.;
RT "Brorin, a novel secreted bone morphogenetic protein antagonist, promotes
RT neurogenesis in mouse neural precursor cells.";
RL J. Biol. Chem. 282:15843-15850(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Mochida Y., Yamauchi M.;
RT "A novel member of cysteine-rich protein family highly expressed in
RT brain.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina, and Spinal cord;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP 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).
RN [8]
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: BMP antagonist which may play a role in neural development.
CC Promotes cell adhesion. {ECO:0000269|PubMed:17400546,
CC ECO:0000269|PubMed:18757743}.
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 VWC2. Alone or in combination,
CC these auxiliary subunits control the gating and pharmacology of the
CC AMPAR complex and profoundly impact their biogenesis and protein
CC processing. {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Synapse {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain (at protein
CC level). It is expressed in the neurons but not the glial cells.
CC {ECO:0000269|PubMed:17400546, ECO:0000269|PubMed:18757743,
CC ECO:0000269|PubMed:22632720}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, predominantly expressed in the
CC developing diencephalon. At 16.5 dpc and 18.5 dpc, expressed in the
CC brain, spinal cord, developing neural tubes and tongue but not in the
CC cerebral cortex. At 16.5 dpc, present in developing oral and tooth germ
CC epithelia (at protein level). {ECO:0000269|PubMed:17400546,
CC ECO:0000269|PubMed:18757743}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25053.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB292670; BAF51550.1; -; mRNA.
DR EMBL; DQ421811; ABD83334.1; -; mRNA.
DR EMBL; AK044771; BAC32080.1; -; mRNA.
DR EMBL; AK141514; BAE24710.1; -; mRNA.
DR EMBL; AL663084; CAI25053.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL663071; CAI25053.2; JOINED; Genomic_DNA.
DR EMBL; AL663071; CAI35949.1; -; Genomic_DNA.
DR EMBL; AL663084; CAI35949.1; JOINED; Genomic_DNA.
DR EMBL; CH466574; EDL40630.1; -; Genomic_DNA.
DR EMBL; CH466574; EDL40631.1; -; Genomic_DNA.
DR EMBL; BC120564; AAI20565.1; -; mRNA.
DR EMBL; BC137825; AAI37826.1; -; mRNA.
DR CCDS; CCDS36111.1; -.
DR RefSeq; NP_796007.1; NM_177033.3.
DR AlphaFoldDB; Q8C8N3; -.
DR SMR; Q8C8N3; -.
DR STRING; 10090.ENSMUSP00000105303; -.
DR PaxDb; Q8C8N3; -.
DR PRIDE; Q8C8N3; -.
DR ProteomicsDB; 297836; -.
DR Antibodypedia; 62692; 60 antibodies from 12 providers.
DR DNASU; 319922; -.
DR Ensembl; ENSMUST00000056344; ENSMUSP00000049692; ENSMUSG00000050830.
DR Ensembl; ENSMUST00000109681; ENSMUSP00000105303; ENSMUSG00000050830.
DR Ensembl; ENSMUST00000129670; ENSMUSP00000128761; ENSMUSG00000050830.
DR GeneID; 319922; -.
DR KEGG; mmu:319922; -.
DR UCSC; uc007iac.1; mouse.
DR CTD; 375567; -.
DR MGI; MGI:2442987; Vwc2.
DR VEuPathDB; HostDB:ENSMUSG00000050830; -.
DR eggNOG; ENOG502QW4Q; Eukaryota.
DR GeneTree; ENSGT00720000108792; -.
DR HOGENOM; CLU_073865_0_0_1; -.
DR InParanoid; Q8C8N3; -.
DR OMA; RHECKQM; -.
DR OrthoDB; 1478107at2759; -.
DR PhylomeDB; Q8C8N3; -.
DR TreeFam; TF329913; -.
DR BioGRID-ORCS; 319922; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8C8N3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C8N3; protein.
DR Bgee; ENSMUSG00000050830; Expressed in medial geniculate body and 147 other tissues.
DR Genevisible; Q8C8N3; 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:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:HGNC-UCL.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:HGNC-UCL.
DR InterPro; IPR042979; VWC2/VWC2L.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46252; PTHR46252; 1.
DR Pfam; PF00093; VWC; 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 Basement membrane; Extracellular matrix; Reference proteome; Repeat;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..324
FT /note="Brorin"
FT /id="PRO_0000307160"
FT DOMAIN 152..211
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 215..273
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 37..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..116
FT /note="Mediates cell adhesion"
FT COMPBIAS 41..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 35383 MW; E6DD3FEB07F91DCB CRC64;
MPSSSAMAVG ALSSSLLVTC CLMVALCSPS IPLEKLAQAP EQPGQEKREH ASRDSPGRVS
ELGRASRDEG SSARDWKSKG SRALSGREAW SKQKQAWAAQ GGSAKAADWQ VRPRGDTPQG
EPPAAAQEAI SLELVPTPEL PEEYAYPDYR GKGCVDESGF VYAIGEKFAP GPSACPCLCT
EEGPLCAQPE CPRLHPRCIH VDNSQCCPQC KEKKNYCEFR GKTYQTLEEF VVSPCERCRC
EANGEVLCTV SACPQTECVD PVYEPDQCCP ICKNGPNCFA ETAVIPAGRE VKTDECTICH
CTYEEGTWRI ERQAMCTRHE CRQM
