SVBP_RAT
ID SVBP_RAT Reviewed; 66 AA.
AC Q4KLG3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Small vasohibin-binding protein {ECO:0000250|UniProtKB:Q8N300};
DE AltName: Full=Coiled coil domain-containing protein 23 {ECO:0000312|RGD:1311232};
GN Name=Svbp {ECO:0000250|UniProtKB:Q8N300};
GN Synonyms=Ccdc23 {ECO:0000312|RGD:1311232};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION.
RX PubMed=30607023; DOI=10.1038/s41436-018-0415-8;
RA Iqbal Z., Tawamie H., Ba W., Reis A., Halak B.A., Sticht H., Uebe S.,
RA Kasri N.N., Riazuddin S., van Bokhoven H., Abou Jamra R.;
RT "Loss of function of SVBP leads to autosomal recessive intellectual
RT disability, microcephaly, ataxia, and hypotonia.";
RL Genet. Med. 21:1790-1796(2019).
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. Plays a role in axon and excitatory synapse
CC formation (PubMed:30607023). {ECO:0000250|UniProtKB:Q8N300,
CC ECO:0000269|PubMed:30607023}.
CC -!- SUBUNIT: Interacts with VASH1 and VASH2.
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}.
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; BC099226; AAH99226.1; -; mRNA.
DR RefSeq; NP_001034081.1; NM_001038992.1.
DR RefSeq; NP_001034083.1; NM_001038994.2.
DR AlphaFoldDB; Q4KLG3; -.
DR SMR; Q4KLG3; -.
DR STRING; 10116.ENSRNOP00000009879; -.
DR PaxDb; Q4KLG3; -.
DR GeneID; 362578; -.
DR KEGG; rno:362578; -.
DR CTD; 374969; -.
DR RGD; 1311232; Svbp.
DR eggNOG; ENOG502S99I; Eukaryota.
DR HOGENOM; CLU_2830589_0_0_1; -.
DR InParanoid; Q4KLG3; -.
DR OrthoDB; 1531949at2759; -.
DR PRO; PR:Q4KLG3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007404; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q4KLG3; baseline and differential.
DR Genevisible; Q4KLG3; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
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:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
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..66
FT /note="Small vasohibin-binding protein"
FT /id="PRO_0000233665"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..52
FT /evidence="ECO:0000255"
SQ SEQUENCE 66 AA; 7836 MW; 9C0F238316F33CC8 CRC64;
MDPPARKEKS KVKEPAFRVE KAKQKSAQQE LKQRQRAEIY ALNRVMTELE QQQFDEFCKQ
MQPPGE