ID VWC2L_MACFA Reviewed; 138 AA. AC Q95K75; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 56. DE RecName: Full=von Willebrand factor C domain-containing protein 2-like; DE Flags: Precursor; GN Name=VWC2L; Synonyms=QtrA-13554; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Temporal cortex; RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K., RA Suzuki Y., Sugano S., Hashimoto K.; RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. 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 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 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Synapse {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB063096; BAB60802.1; -; mRNA. DR AlphaFoldDB; Q95K75; -. DR STRING; 9541.ENSMFAP00000009893; -. DR eggNOG; ENOG502RAAU; Eukaryota. DR Proteomes; UP000233100; Unplaced. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR InterPro; IPR042979; VWC2/VWC2L. DR PANTHER; PTHR46252; BRORIN FAMILY MEMBER; 1. DR PANTHER; PTHR46252:SF2; VON WILLEBRAND FACTOR C DOMAIN-CONTAINING PROTEIN 2-LIKE; 1. PE 2: Evidence at transcript level; KW Developmental protein; Reference proteome; Secreted; Signal; Synapse. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..138 FT /note="von Willebrand factor C domain-containing protein 2- FT like" FT /id="PRO_0000348061" FT DOMAIN 51..110 FT /note="VWFC" SQ SEQUENCE 138 AA; 15382 MW; A6F3AB068821A555 CRC64; MALHIHEACI LLLVIPGLVT SAAISHEDYP ADEGDQISSN DNLIFDDYRG KGCVDDSGFV YKLGERFFPG HSNCPCVCAL DGPVCDQPEC PKIHPKCTKV EHNGCCPECK EVKNFCEYHG KNYKILEEFK VCVTLHTY //