GenomeNet

Database: UniProt
Entry: Q8C8N3
LinkDB: Q8C8N3
Original site: Q8C8N3 
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   10-APR-2019, entry version 113.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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,
RT   promotes 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.,
RA   Kiyozumi D., Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S.,
RA   Kawai J., Sugiura N., 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.,
RA   Muller C.S., Bildl W., Baehrens D., Huber B., Kulik A., Klocker N.,
RA   Schulte U., Fakler B.;
RT   "High-resolution proteomics unravel architecture and molecular
RT   diversity of native AMPA receptor complexes.";
RL   Neuron 74:621-633(2012).
CC   -!- FUNCTION: BMP antagonist which may play a role in neural
CC       development. 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
CC       proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary
CC       subunits arranged in a twofold symmetry. One of the two pairs of
CC       distinct binding sites is occupied either by CNIH2, CNIH3 or
CC       CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8
CC       or GSG1L. This inner core of AMPAR complex is complemented by
CC       outer core constituents binding directly to the GluA/GRIA proteins
CC       at sites distinct from the interaction sites of the inner core
CC       constituents. Outer core constituents include at least PRRT1,
CC       PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner
CC       and outer core serve as a platform for other, more peripherally
CC       associated AMPAR constituents, including VWC2. 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, extracellular space, extracellular
CC       matrix, basement membrane. Cell junction, synapse {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain (at
CC       protein level). It is expressed in the neurons but not the glial
CC       cells. {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
CC       the brain, spinal cord, developing neural tubes and tongue but not
CC       in the cerebral cortex. At 16.5 dpc, present in developing oral
CC       and tooth germ epithelia (at protein level).
CC       {ECO:0000269|PubMed:17400546, ECO:0000269|PubMed:18757743}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI25053.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Mm.337851; -.
DR   UniGene; Mm.487612; -.
DR   ProteinModelPortal; Q8C8N3; -.
DR   SMR; Q8C8N3; -.
DR   STRING; 10090.ENSMUSP00000105303; -.
DR   PaxDb; Q8C8N3; -.
DR   PRIDE; Q8C8N3; -.
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   eggNOG; ENOG410IK6F; Eukaryota.
DR   eggNOG; ENOG410YDUI; LUCA.
DR   GeneTree; ENSGT00720000108792; -.
DR   HOGENOM; HOG000036086; -.
DR   HOVERGEN; HBG094842; -.
DR   InParanoid; Q8C8N3; -.
DR   OMA; CTRHECK; -.
DR   OrthoDB; 1478107at2759; -.
DR   PhylomeDB; Q8C8N3; -.
DR   TreeFam; TF329913; -.
DR   PRO; PR:Q8C8N3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000050830; Expressed in 184 organ(s), highest expression level in brain.
DR   Genevisible; Q8C8N3; MM.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:HGNC.
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.
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.
DR   InterPro; IPR001007; VWF_dom.
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; Cell junction; Complete proteome;
KW   Extracellular matrix; Reference proteome; Repeat; Secreted; Signal;
KW   Synapse.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28    324       Brorin.
FT                                /FTId=PRO_0000307160.
FT   DOMAIN      152    211       VWFC 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      215    273       VWFC 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   MOTIF       114    116       Mediates cell adhesion.
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
//
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