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SVBP_MOUSE
ID   SVBP_MOUSE              Reviewed;          66 AA.
AC   Q99LQ4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Small vasohibin-binding protein {ECO:0000303|PubMed:20736312};
DE   AltName: Full=Coiled coil domain-containing protein 23 {ECO:0000312|MGI:MGI:1916466};
GN   Name=Svbp {ECO:0000303|PubMed:20736312};
GN   Synonyms=Ccdc23 {ECO:0000312|MGI:MGI:1916466};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20736312; DOI=10.1242/jcs.067538;
RA   Suzuki Y., Kobayashi M., Miyashita H., Ohta H., Sonoda H., Sato Y.;
RT   "Isolation of a small vasohibin-binding protein (SVBP) and its role in
RT   vasohibin secretion.";
RL   J. Cell Sci. 123:3094-3101(2010).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH VASH1 AND VASH2.
RX   PubMed=29146868; DOI=10.1126/science.aao4165;
RA   Aillaud C., Bosc C., Peris L., Bosson A., Heemeryck P., Van Dijk J.,
RA   Le Friec J., Boulan B., Vossier F., Sanman L.E., Syed S., Amara N.,
RA   Coute Y., Lafanechere L., Denarier E., Delphin C., Pelletier L.,
RA   Humbert S., Bogyo M., Andrieux A., Rogowski K., Moutin M.J.;
RT   "Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron
RT   differentiation.";
RL   Science 358:1448-1453(2017).
RN   [5]
RP   INTERACTION WITH VASH2.
RX   PubMed=31324789; DOI=10.1038/s41467-019-11277-8;
RA   Zhou C., Yan L., Zhang W.H., Liu Z.;
RT   "Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer.";
RL   Nat. Commun. 10:3212-3212(2019).
RN   [6]
RP   FUNCTION.
RX   PubMed=31235911; DOI=10.1038/s41594-019-0241-y;
RA   Wang N., Bosc C., Ryul Choi S., Boulan B., Peris L., Olieric N., Bao H.,
RA   Krichen F., Chen L., Andrieux A., Olieric V., Moutin M.J., Steinmetz M.O.,
RA   Huang H.;
RT   "Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme
RT   complex.";
RL   Nat. Struct. Mol. Biol. 26:571-582(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 (PubMed:29146868). Also required to enhance the
CC       solubility and secretion of VASH1 and VASH2 (By similarity). Plays a
CC       role in axon and excitatory synapse formation (PubMed:31235911).
CC       {ECO:0000250|UniProtKB:Q8N300, ECO:0000269|PubMed:29146868,
CC       ECO:0000269|PubMed:31235911}.
CC   -!- SUBUNIT: Interacts with VASH1 and VASH2. {ECO:0000269|PubMed:29146868,
CC       ECO:0000269|PubMed:31324789}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20736312}. Secreted
CC       {ECO:0000269|PubMed:20736312}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8N300}. Note=Detected both intracellularly and
CC       extracellularly (PubMed:20736312). Within cells, localizes mainly to
CC       the apical part of the cell (PubMed:20736312).
CC       {ECO:0000269|PubMed:20736312}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in bone marrow, spleen and testis.
CC       {ECO:0000269|PubMed:20736312}.
CC   -!- SIMILARITY: Belongs to the SVBP family. {ECO:0000305}.
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DR   EMBL; AK010418; BAC25297.1; -; mRNA.
DR   EMBL; BC002274; AAH02274.1; -; mRNA.
DR   CCDS; CCDS38858.1; -.
DR   RefSeq; NP_077782.1; NM_024462.2.
DR   AlphaFoldDB; Q99LQ4; -.
DR   SMR; Q99LQ4; -.
DR   STRING; 10090.ENSMUSP00000095518; -.
DR   PhosphoSitePlus; Q99LQ4; -.
DR   EPD; Q99LQ4; -.
DR   MaxQB; Q99LQ4; -.
DR   PaxDb; Q99LQ4; -.
DR   PRIDE; Q99LQ4; -.
DR   ProteomicsDB; 254723; -.
DR   Antibodypedia; 2034; 62 antibodies from 12 providers.
DR   DNASU; 69216; -.
DR   Ensembl; ENSMUST00000030395; ENSMUSP00000030395; ENSMUSG00000028643.
DR   GeneID; 69216; -.
DR   KEGG; mmu:69216; -.
DR   UCSC; uc008ulk.2; mouse.
DR   CTD; 374969; -.
DR   MGI; MGI:1916466; Svbp.
DR   VEuPathDB; HostDB:ENSMUSG00000028643; -.
DR   eggNOG; ENOG502S99I; Eukaryota.
DR   GeneTree; ENSGT00390000006113; -.
DR   HOGENOM; CLU_2830589_0_0_1; -.
DR   InParanoid; Q99LQ4; -.
DR   OMA; TFCKQMQ; -.
DR   PhylomeDB; Q99LQ4; -.
DR   BioGRID-ORCS; 69216; 1 hit in 37 CRISPR screens.
DR   ChiTaRS; Svbp; mouse.
DR   PRO; PR:Q99LQ4; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q99LQ4; protein.
DR   Bgee; ENSMUSG00000028643; Expressed in embryonic brain and 251 other tissues.
DR   ExpressionAtlas; Q99LQ4; baseline and differential.
DR   Genevisible; Q99LQ4; MM.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
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; IMP:UniProtKB.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR   GO; GO:0009306; P:protein secretion; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IDA: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   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Secreted.
FT   CHAIN           1..66
FT                   /note="Small vasohibin-binding protein"
FT                   /id="PRO_0000233664"
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
 
 
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