SVBP_TAEGU
ID SVBP_TAEGU Reviewed; 68 AA.
AC B5FZ42;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Small vasohibin-binding protein {ECO:0000250|UniProtKB:Q8N300};
DE AltName: Full=Coiled-coil domain-containing protein 23 {ECO:0000250|UniProtKB:Q8N300};
GN Name=SVBP {ECO:0000250|UniProtKB:Q8N300};
GN Synonyms=CCDC23 {ECO:0000250|UniProtKB:Q8N300};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
CC -!- FUNCTION: Enhances the tyrosine carboxypeptidase activity of vash1 and
CC vash2, thereby promoting the removal of the C-terminal tyrosine residue
CC of alpha-tubulin. Also required to enhance the solubility and secretion
CC of vash1 and vash2. May play a role in axon and excitatory synapse
CC formation (By similarity). {ECO:0000250|UniProtKB:Q4KLG3,
CC ECO:0000250|UniProtKB:Q8N300}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99LQ4}.
CC Secreted {ECO:0000250|UniProtKB:Q99LQ4}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8N300}. Note=Detected both intracellularly and
CC extracellularly. Within cells, localizes mainly to the apical part of
CC the cell. {ECO:0000250|UniProtKB:Q99LQ4}.
CC -!- SIMILARITY: Belongs to the SVBP family. {ECO:0000305}.
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DR EMBL; DQ214301; ACH44303.1; -; mRNA.
DR EMBL; FJ154882; ACI04464.1; -; mRNA.
DR RefSeq; NP_001232099.1; NM_001245170.1.
DR AlphaFoldDB; B5FZ42; -.
DR SMR; B5FZ42; -.
DR STRING; 59729.ENSTGUP00000032171; -.
DR Ensembl; ENSTGUT00000032326; ENSTGUP00000032171; ENSTGUG00000019639.
DR GeneID; 100190225; -.
DR KEGG; tgu:100190225; -.
DR CTD; 374969; -.
DR GeneTree; ENSGT00390000006113; -.
DR InParanoid; B5FZ42; -.
DR Proteomes; UP000007754; Chromosome 21.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:1905048; P:regulation of metallopeptidase activity; ISS:UniProtKB.
DR InterPro; IPR031378; SVBP.
DR PANTHER; PTHR34762; PTHR34762; 1.
DR Pfam; PF15674; CCDC23; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Secreted.
FT CHAIN 1..68
FT /note="Small vasohibin-binding protein"
FT /id="PRO_0000359891"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..54
FT /evidence="ECO:0000255"
SQ SEQUENCE 68 AA; 7862 MW; 21A68059D1028EA5 CRC64;
MDPGAGARKE RPKPREPAAR LEKAKQRSAQ QELKQRQRAE IYALNRVMTE LEQQQFDSFC
KQMQGSGE
