ID   VWC2L_HUMAN             Reviewed;         222 AA.
AC   B2RUY7; A6NC69; B2RUW7; B7X8X1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   13-FEB-2019, entry version 76.
DE   RecName: Full=von Willebrand factor C domain-containing protein 2-like;
DE   AltName: Full=Brorin-like;
DE   Flags: Precursor;
GN   Name=VWC2L;
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] (ISOFORM 1).
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] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Mochida Y., Yamauchi M.;
RT   "A novel cysteine-knot protein regulates matrix mineralization.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain cortex;
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: May play a role in neurogenesis. May play a role in bone
CC       differentiation and matrix mineralization. {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 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 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q13643:FHL3; NbExp=4; IntAct=EBI-11747707, EBI-741101;
CC       P49639:HOXA1; NbExp=4; IntAct=EBI-11747707, EBI-740785;
CC       Q5TA76:LCE3A; NbExp=4; IntAct=EBI-11747707, EBI-9394625;
CC       P32242:OTX1; NbExp=4; IntAct=EBI-11747707, EBI-740446;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell junction,
CC       synapse {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B2RUY7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B2RUY7-2; Sequence=VSP_035088, VSP_035089;
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DR   EMBL; AB374231; BAH04176.1; -; mRNA.
DR   EMBL; EU541473; ACD62527.1; -; mRNA.
DR   EMBL; AC107218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC146903; AAI46904.1; -; mRNA.
DR   EMBL; BC146911; AAI46912.1; -; mRNA.
DR   EMBL; BC146931; AAI46932.1; -; mRNA.
DR   EMBL; BC146935; AAI46936.1; -; mRNA.
DR   CCDS; CCDS46509.1; -. [B2RUY7-1]
DR   RefSeq; NP_001073969.1; NM_001080500.3. [B2RUY7-1]
DR   UniGene; Hs.534834; -.
DR   ProteinModelPortal; B2RUY7; -.
DR   BioGrid; 135334; 13.
DR   IntAct; B2RUY7; 28.
DR   STRING; 9606.ENSP00000308976; -.
DR   iPTMnet; B2RUY7; -.
DR   PhosphoSitePlus; B2RUY7; -.
DR   BioMuta; VWC2L; -.
DR   PaxDb; B2RUY7; -.
DR   PRIDE; B2RUY7; -.
DR   ProteomicsDB; 3456; -.
DR   ProteomicsDB; 3457; -. [B2RUY7-2]
DR   Ensembl; ENST00000312504; ENSP00000308976; ENSG00000174453. [B2RUY7-1]
DR   GeneID; 402117; -.
DR   KEGG; hsa:402117; -.
DR   UCSC; uc002vet.3; human. [B2RUY7-1]
DR   CTD; 402117; -.
DR   DisGeNET; 402117; -.
DR   EuPathDB; HostDB:ENSG00000174453.9; -.
DR   GeneCards; VWC2L; -.
DR   HGNC; HGNC:37203; VWC2L.
DR   HPA; HPA044815; -.
DR   HPA; HPA059414; -.
DR   neXtProt; NX_B2RUY7; -.
DR   OpenTargets; ENSG00000174453; -.
DR   PharmGKB; PA165697841; -.
DR   eggNOG; ENOG410IHPX; Eukaryota.
DR   eggNOG; ENOG410XTA9; LUCA.
DR   GeneTree; ENSGT00720000108792; -.
DR   HOGENOM; HOG000036086; -.
DR   HOVERGEN; HBG068398; -.
DR   InParanoid; B2RUY7; -.
DR   OMA; CTICRCH; -.
DR   OrthoDB; 1478107at2759; -.
DR   PhylomeDB; B2RUY7; -.
DR   TreeFam; TF329913; -.
DR   GenomeRNAi; 402117; -.
DR   PRO; PR:B2RUY7; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000174453; Expressed in 22 organ(s), highest expression level in hypothalamus.
DR   ExpressionAtlas; B2RUY7; baseline and differential.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   InterPro; IPR001007; VWF_dom.
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; Cell junction; Complete proteome;
KW   Developmental protein; Reference proteome; Repeat; Secreted; Signal;
KW   Synapse.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    222       von Willebrand factor C domain-containing
FT                                protein 2-like.
FT                                /FTId=PRO_0000348060.
FT   DOMAIN       51    110       VWFC 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      114    172       VWFC 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   VAR_SEQ     131    138       PSPCEWCR -> VCVTLHIY (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_035088.
FT   VAR_SEQ     139    222       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_035089.
SQ   SEQUENCE   222 AA;  24570 MW;  7047CE3CBA835B54 CRC64;
     MALHIHEACI LLLVIPGLVT SAAISHEDYP ADEGDQISSN DNLIFDDYRG KGCVDDSGFV
     YKLGERFFPG HSNCPCVCAL DGPVCDQPEC PKIHPKCTKV EHNGCCPECK EVKNFCEYHG
     KNYKILEEFK PSPCEWCRCE PSNEVHCVVA DCAVPECVNP VYEPEQCCPV CKNGPNCFAG
     TTIIPAGIEV KVDECNICHC HNGDWWKPAQ CSKRECQGKQ TV
//