GenomeNet

Database: UniProt
Entry: Q2TAL6
LinkDB: Q2TAL6
Original site: Q2TAL6 
ID   VWC2_HUMAN              Reviewed;         325 AA.
AC   Q2TAL6; Q6UXE2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   13-FEB-2019, entry version 103.
DE   RecName: Full=Brorin;
DE   AltName: Full=Brain-specific chordin-like protein;
DE   AltName: Full=von Willebrand factor C domain-containing protein 2;
DE   Flags: Precursor;
GN   Name=VWC2; ORFNames=UNQ739/PRO1434;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: BMP antagonist which may play a role in neural
CC       development. Promotes cell adhesion (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6UY14-3:ADAMTSL4; NbExp=4; IntAct=EBI-11957238, EBI-10173507;
CC       P49639:HOXA1; NbExp=4; IntAct=EBI-11957238, EBI-740785;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250}. Cell junction, synapse
CC       {ECO:0000250}.
DR   EMBL; AB292671; BAF51551.1; -; mRNA.
DR   EMBL; AY358393; AAQ88759.1; -; mRNA.
DR   EMBL; CH471128; EAW60985.1; -; Genomic_DNA.
DR   EMBL; CH236955; EAL23904.1; -; Genomic_DNA.
DR   EMBL; BC110857; AAI10858.1; -; mRNA.
DR   CCDS; CCDS5508.1; -.
DR   RefSeq; NP_940972.2; NM_198570.4.
DR   UniGene; Hs.629302; -.
DR   UniGene; Hs.629814; -.
DR   UniGene; Hs.657556; -.
DR   ProteinModelPortal; Q2TAL6; -.
DR   SMR; Q2TAL6; -.
DR   BioGrid; 131984; 4.
DR   IntAct; Q2TAL6; 57.
DR   STRING; 9606.ENSP00000341819; -.
DR   BioMuta; VWC2; -.
DR   DMDM; 121941771; -.
DR   PaxDb; Q2TAL6; -.
DR   PeptideAtlas; Q2TAL6; -.
DR   PRIDE; Q2TAL6; -.
DR   ProteomicsDB; 61467; -.
DR   Ensembl; ENST00000340652; ENSP00000341819; ENSG00000188730.
DR   GeneID; 375567; -.
DR   KEGG; hsa:375567; -.
DR   UCSC; uc003tot.2; human.
DR   CTD; 375567; -.
DR   EuPathDB; HostDB:ENSG00000188730.4; -.
DR   GeneCards; VWC2; -.
DR   H-InvDB; HIX0033600; -.
DR   HGNC; HGNC:30200; VWC2.
DR   HPA; HPA055243; -.
DR   MIM; 611108; gene.
DR   neXtProt; NX_Q2TAL6; -.
DR   OpenTargets; ENSG00000188730; -.
DR   PharmGKB; PA147357154; -.
DR   eggNOG; ENOG410IK6F; Eukaryota.
DR   eggNOG; ENOG410YDUI; LUCA.
DR   GeneTree; ENSGT00720000108792; -.
DR   HOGENOM; HOG000036086; -.
DR   HOVERGEN; HBG094842; -.
DR   InParanoid; Q2TAL6; -.
DR   OMA; CTRHECK; -.
DR   OrthoDB; 1478107at2759; -.
DR   PhylomeDB; Q2TAL6; -.
DR   TreeFam; TF329913; -.
DR   GenomeRNAi; 375567; -.
DR   PRO; PR:Q2TAL6; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000188730; Expressed in 66 organ(s), highest expression level in cerebellar hemisphere.
DR   Genevisible; Q2TAL6; HS.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; ISS:HGNC.
DR   GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:HGNC.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS: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; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Signal; Synapse.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28    325       Brorin.
FT                                /FTId=PRO_0000307159.
FT   DOMAIN      153    212       VWFC 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      216    274       VWFC 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   MOTIF       114    116       Mediates cell adhesion. {ECO:0000250}.
FT   COMPBIAS    120    127       Poly-Ala.
FT   VARIANT     120    120       A -> G (in dbSNP:rs769604).
FT                                /FTId=VAR_035371.
FT   CONFLICT     52     52       S -> T (in Ref. 1; BAF51551 and 2;
FT                                AAQ88759). {ECO:0000305}.
SQ   SEQUENCE   325 AA;  35282 MW;  A38B673AB376B64D CRC64;
     MPSSTAMAVG ALSSSLLVTC CLMVALCSPS IPLEKLAQAP EQPGQEKREH ASRDGPGRVN
     ELGRPARDEG GSGRDWKSKS GRGLAGREPW SKLKQAWVSQ GGGAKAGDLQ VRPRGDTPQA
     EALAAAAQDA IGPELAPTPE PPEEYVYPDY RGKGCVDESG FVYAIGEKFA PGPSACPCLC
     TEEGPLCAQP ECPRLHPRCI HVDTSQCCPQ CKERKNYCEF RGKTYQTLEE FVVSPCERCR
     CEANGEVLCT VSACPQTECV DPVYEPDQCC PICKNGPNCF AETAVIPAGR EVKTDECTIC
     HCTYEEGTWR IERQAMCTRH ECRQM
//
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