SVBP_DANRE
ID SVBP_DANRE Reviewed; 65 AA.
AC P0C8M3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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}.
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 RefSeq; NP_001189361.1; NM_001202432.2.
DR AlphaFoldDB; P0C8M3; -.
DR SMR; P0C8M3; -.
DR STRING; 7955.ENSDARP00000108444; -.
DR PaxDb; P0C8M3; -.
DR Ensembl; ENSDART00000167495; ENSDARP00000136802; ENSDARG00000102305.
DR GeneID; 798425; -.
DR KEGG; dre:798425; -.
DR CTD; 374969; -.
DR ZFIN; ZDB-GENE-140106-191; svbp.
DR eggNOG; ENOG502S99I; Eukaryota.
DR GeneTree; ENSGT00390000006113; -.
DR HOGENOM; CLU_2830589_0_0_1; -.
DR InParanoid; P0C8M3; -.
DR OMA; KQMQSQA; -.
DR OrthoDB; 1606567at2759; -.
DR PhylomeDB; P0C8M3; -.
DR TreeFam; TF344015; -.
DR PRO; PR:P0C8M3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000102305; Expressed in somite and 26 other tissues.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
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:0031397; P:negative regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
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..65
FT /note="Small vasohibin-binding protein"
FT /id="PRO_0000359892"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..51
FT /evidence="ECO:0000255"
SQ SEQUENCE 65 AA; 7762 MW; 6DC0A616D51ADFF0 CRC64;
MEPACRKDKQ KQQTPTRGDR TKQKTAQQEL KQRQRAEIYA LNKVMTELEQ QQFEAFCKQM
QSQSE
