SVBP_HUMAN
ID SVBP_HUMAN Reviewed; 66 AA.
AC Q8N300; A8K5P1; D3DPW7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Small vasohibin-binding protein {ECO:0000303|PubMed:20736312};
DE AltName: Full=Coiled coil domain-containing protein 23 {ECO:0000312|HGNC:HGNC:29204};
GN Name=SVBP {ECO:0000303|PubMed:20736312, ECO:0000312|HGNC:HGNC:29204};
GN Synonyms=CCDC23 {ECO:0000312|HGNC:HGNC:29204};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP FUNCTION, AND INTERACTION WITH VASH1 AND VASH2.
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 [6]
RP FUNCTION, AND INTERACTION WITH VASH1.
RX PubMed=27879017; DOI=10.1002/pro.3089;
RA Kadonosono T., Yimchuen W., Tsubaki T., Shiozawa T., Suzuki Y.,
RA Kuchimaru T., Sato Y., Kizaka-Kondoh S.;
RT "Domain architecture of vasohibins required for their chaperone-dependent
RT unconventional extracellular release.";
RL Protein Sci. 26:452-463(2017).
RN [7]
RP FUNCTION, AND INTERACTION WITH VASH1 AND VASH2.
RX PubMed=29146869; DOI=10.1126/science.aao5676;
RA Nieuwenhuis J., Adamopoulos A., Bleijerveld O.B., Mazouzi A., Stickel E.,
RA Celie P., Altelaar M., Knipscheer P., Perrakis A., Blomen V.A.,
RA Brummelkamp T.R.;
RT "Vasohibins encode tubulin detyrosinating activity.";
RL Science 358:1453-1456(2017).
RN [8] {ECO:0007744|PDB:6J7B, ECO:0007744|PDB:6J8F, ECO:0007744|PDB:6J8N, ECO:0007744|PDB:6J91, ECO:0007744|PDB:6J9H}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 20-50 IN COMPLEX WITH VASH1,
RP INTERACTION WITH VASH1, MUTAGENESIS OF 35-GLN-ARG-36; 39-ILE-TYR-40;
RP 42-LEU-ASN-43 AND 45-VAL-MET-46, AND FUNCTION.
RX PubMed=31171830; DOI=10.1038/s41422-019-0187-y;
RA Liao S., Rajendraprasad G., Wang N., Eibes S., Gao J., Yu H., Wu G., Tu X.,
RA Huang H., Barisic M., Xu C.;
RT "Molecular basis of vasohibins-mediated detyrosination and its impact on
RT spindle function and mitosis.";
RL Cell Res. 29:533-547(2019).
RN [9] {ECO:0007744|PDB:6JZC, ECO:0007744|PDB:6JZD, ECO:0007744|PDB:6JZE}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-60 IN COMPLEX WITH VASH2,
RP INTERACTION WITH VASH2, AND FUNCTION.
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 [10] {ECO:0007744|PDB:6NVQ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 23-56 IN COMPLEX WITH VASH1,
RP INTERACTION WITH VASH1, FUNCTION, AND MUTAGENESIS OF LYS-32; ARG-34;
RP GLN-35; ARG-36; TYR-40; ASN-43 AND THR-47.
RX PubMed=31270470; DOI=10.1038/s41594-019-0254-6;
RA Adamopoulos A., Landskron L., Heidebrecht T., Tsakou F., Bleijerveld O.B.,
RA Altelaar M., Nieuwenhuis J., Celie P.H.N., Brummelkamp T.R., Perrakis A.;
RT "Crystal structure of the tubulin tyrosine carboxypeptidase complex VASH1-
RT SVBP.";
RL Nat. Struct. Mol. Biol. 26:567-570(2019).
RN [11] {ECO:0007744|PDB:6QBY}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 26-58 IN COMPLEX WITH VASH2 AND
RP TUBULIN PEPTIDE, INTERACTION WITH VASH2, FUNCTION, MUTAGENESIS OF
RP 35-GLN-ARG-36; 39-ILE-TYR-40; 42-LEU-ASN-43; 45-VAL-MET-46 AND
RP 50-GLU--PHE-54, AND SUBCELLULAR LOCATION.
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).
RN [12] {ECO:0007744|PDB:6OCF, ECO:0007744|PDB:6OCG, ECO:0007744|PDB:6OCH}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 18-66 IN COMPLEX WITH VASH1,
RP INTERACTION WITH VASH1, FUNCTION, AND MUTAGENESIS OF 39-ILE--LEU-42; ILE-39
RP AND LEU-42.
RX PubMed=31235910; DOI=10.1038/s41594-019-0242-x;
RA Li F., Hu Y., Qi S., Luo X., Yu H.;
RT "Structural basis of tubulin detyrosination by vasohibins.";
RL Nat. Struct. Mol. Biol. 26:583-591(2019).
RN [13]
RP INVOLVEMENT IN NEDAHM, FUNCTION, VARIANT NEDAHM 28-GLN--GLU-66 DEL, AND
RP CHARACTERIZATION OF VARIANT NEDAHM 28-GLN--GLU-66 DEL.
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 (PubMed:29146869, PubMed:31270470, PubMed:31235911,
CC PubMed:31324789, PubMed:31171830, PubMed:31235910). This activity is
CC critical for spindle function and accurate chromosome segregation
CC during mitosis since microtuble detyronisation regulates mitotic
CC spindle length and postioning (PubMed:31171830). Also required to
CC enhance the solubility and secretion of VASH1 and VASH2
CC (PubMed:20736312, PubMed:27879017, PubMed:30607023). Plays a role in
CC axon and excitatory synapse formation (PubMed:31235911).
CC {ECO:0000269|PubMed:20736312, ECO:0000269|PubMed:27879017,
CC ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:30607023,
CC ECO:0000269|PubMed:31171830, ECO:0000269|PubMed:31235910,
CC ECO:0000269|PubMed:31235911, ECO:0000269|PubMed:31270470,
CC ECO:0000269|PubMed:31324789}.
CC -!- SUBUNIT: Interacts with VASH1 and VASH2. {ECO:0000269|PubMed:20736312,
CC ECO:0000269|PubMed:27879017, ECO:0000269|PubMed:29146869,
CC ECO:0000269|PubMed:31171830, ECO:0000269|PubMed:31235910,
CC ECO:0000269|PubMed:31235911, ECO:0000269|PubMed:31270470,
CC ECO:0000269|PubMed:31324789}.
CC -!- INTERACTION:
CC Q8N300; Q7L8A9-1: VASH1; NbExp=2; IntAct=EBI-21497577, EBI-21497569;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99LQ4}.
CC Secreted {ECO:0000250|UniProtKB:Q99LQ4}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:31235911}. Note=Detected both intracellularly and
CC extracellularly (By similarity). Within cells, localizes mainly to the
CC apical part of the cell (By similarity).
CC {ECO:0000250|UniProtKB:Q99LQ4}.
CC -!- DISEASE: Neurodevelopmental disorder with ataxia, hypotonia, and
CC microcephaly (NEDAHM) [MIM:618569]: An autosomal recessive
CC neurodevelopmental disorder characterized by intellectual disability,
CC microcephaly, ataxia, and muscular hypotonia.
CC {ECO:0000269|PubMed:30607023}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SVBP family. {ECO:0000305}.
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DR EMBL; AK291356; BAF84045.1; -; mRNA.
DR EMBL; AC098484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07134.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07135.1; -; Genomic_DNA.
DR EMBL; BC029427; AAH29427.1; -; mRNA.
DR CCDS; CCDS474.1; -.
DR RefSeq; NP_955374.1; NM_199342.3.
DR RefSeq; XP_016856715.1; XM_017001226.1.
DR PDB; 6J4O; X-ray; 2.30 A; B=1-66.
DR PDB; 6J4P; X-ray; 1.60 A; B=1-66.
DR PDB; 6J4Q; X-ray; 2.70 A; B/D/G/K=1-66.
DR PDB; 6J4S; X-ray; 2.80 A; B=1-66.
DR PDB; 6J4U; X-ray; 2.00 A; B=1-66.
DR PDB; 6J4V; X-ray; 2.10 A; B=1-66.
DR PDB; 6J7B; X-ray; 1.62 A; B=1-52.
DR PDB; 6J8F; X-ray; 2.28 A; A=3-48.
DR PDB; 6J8N; X-ray; 1.95 A; A/C=1-66.
DR PDB; 6J8O; X-ray; 1.85 A; A=3-49.
DR PDB; 6J91; X-ray; 3.50 A; A=1-66.
DR PDB; 6J9H; X-ray; 2.31 A; A/C=1-66.
DR PDB; 6JZC; X-ray; 2.20 A; C/D=1-66.
DR PDB; 6JZD; X-ray; 2.48 A; B=1-66.
DR PDB; 6JZE; X-ray; 2.51 A; B=1-66.
DR PDB; 6K81; X-ray; 2.28 A; B=1-66.
DR PDB; 6LPG; X-ray; 2.30 A; B=2-66.
DR PDB; 6NVQ; X-ray; 2.10 A; B=1-66.
DR PDB; 6OCF; X-ray; 2.10 A; B=18-66.
DR PDB; 6OCG; X-ray; 1.83 A; B=26-51.
DR PDB; 6OCH; X-ray; 2.00 A; B/D=25-52.
DR PDB; 6QBY; X-ray; 2.09 A; B/D=1-66.
DR PDB; 6WSL; EM; 3.10 A; D/H=1-66.
DR PDBsum; 6J4O; -.
DR PDBsum; 6J4P; -.
DR PDBsum; 6J4Q; -.
DR PDBsum; 6J4S; -.
DR PDBsum; 6J4U; -.
DR PDBsum; 6J4V; -.
DR PDBsum; 6J7B; -.
DR PDBsum; 6J8F; -.
DR PDBsum; 6J8N; -.
DR PDBsum; 6J8O; -.
DR PDBsum; 6J91; -.
DR PDBsum; 6J9H; -.
DR PDBsum; 6JZC; -.
DR PDBsum; 6JZD; -.
DR PDBsum; 6JZE; -.
DR PDBsum; 6K81; -.
DR PDBsum; 6LPG; -.
DR PDBsum; 6NVQ; -.
DR PDBsum; 6OCF; -.
DR PDBsum; 6OCG; -.
DR PDBsum; 6OCH; -.
DR PDBsum; 6QBY; -.
DR PDBsum; 6WSL; -.
DR AlphaFoldDB; Q8N300; -.
DR SMR; Q8N300; -.
DR BioGRID; 131942; 1.
DR IntAct; Q8N300; 1.
DR STRING; 9606.ENSP00000361599; -.
DR iPTMnet; Q8N300; -.
DR MetOSite; Q8N300; -.
DR PhosphoSitePlus; Q8N300; -.
DR BioMuta; SVBP; -.
DR EPD; Q8N300; -.
DR jPOST; Q8N300; -.
DR MassIVE; Q8N300; -.
DR MaxQB; Q8N300; -.
DR PaxDb; Q8N300; -.
DR PeptideAtlas; Q8N300; -.
DR PRIDE; Q8N300; -.
DR ProteomicsDB; 71745; -.
DR Antibodypedia; 2034; 62 antibodies from 12 providers.
DR DNASU; 374969; -.
DR Ensembl; ENST00000372521.9; ENSP00000361599.4; ENSG00000177868.12.
DR Ensembl; ENST00000372522.5; ENSP00000361600.1; ENSG00000177868.12.
DR GeneID; 374969; -.
DR KEGG; hsa:374969; -.
DR MANE-Select; ENST00000372521.9; ENSP00000361599.4; NM_199342.4; NP_955374.1.
DR UCSC; uc001cib.3; human.
DR CTD; 374969; -.
DR DisGeNET; 374969; -.
DR GeneCards; SVBP; -.
DR HGNC; HGNC:29204; SVBP.
DR HPA; ENSG00000177868; Low tissue specificity.
DR MalaCards; SVBP; -.
DR MIM; 617853; gene.
DR MIM; 618569; phenotype.
DR neXtProt; NX_Q8N300; -.
DR OpenTargets; ENSG00000177868; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA142672181; -.
DR VEuPathDB; HostDB:ENSG00000177868; -.
DR eggNOG; ENOG502S99I; Eukaryota.
DR GeneTree; ENSGT00390000006113; -.
DR HOGENOM; CLU_2830589_0_0_1; -.
DR InParanoid; Q8N300; -.
DR OMA; TFCKQMQ; -.
DR OrthoDB; 1606567at2759; -.
DR PhylomeDB; Q8N300; -.
DR TreeFam; TF344015; -.
DR PathwayCommons; Q8N300; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q8N300; -.
DR BioGRID-ORCS; 374969; 151 hits in 1053 CRISPR screens.
DR ChiTaRS; SVBP; human.
DR GenomeRNAi; 374969; -.
DR Pharos; Q8N300; Tbio.
DR PRO; PR:Q8N300; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N300; protein.
DR Bgee; ENSG00000177868; Expressed in cortical plate and 185 other tissues.
DR Genevisible; Q8N300; HS.
DR GO; GO:0045177; C:apical part of cell; IDA: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; IDA:UniProtKB.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IGI:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0009306; P:protein secretion; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:1905048; P:regulation of metallopeptidase activity; IMP:UniProtKB.
DR InterPro; IPR031378; SVBP.
DR PANTHER; PTHR34762; PTHR34762; 1.
DR Pfam; PF15674; CCDC23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Intellectual disability; Reference proteome; Secreted.
FT CHAIN 1..66
FT /note="Small vasohibin-binding protein"
FT /id="PRO_0000233663"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..52
FT /evidence="ECO:0000255"
FT VARIANT 28..66
FT /note="Missing (in NEDAHM; probably not expressed at
FT protein level; impaired VASH1 secretion and solubility)"
FT /evidence="ECO:0000269|PubMed:30607023"
FT /id="VAR_083027"
FT MUTAGEN 32
FT /note="K->E: Decreased VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 34
FT /note="R->E: No effect on VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 35..36
FT /note="QR->AA: Strongly decreased interaction with VASH1.
FT Decreased VASH1 tyrosine carboxypeptidase activity on
FT alpha-tubulin. Strongly decreased interaction with VASH2.
FT Decreased VASH2 tyrosine carboxypeptidase activity on
FT alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31171830,
FT ECO:0000269|PubMed:31235911"
FT MUTAGEN 35
FT /note="Q->A: Decreased VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 36
FT /note="R->E: Decreased VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 39..42
FT /note="IYAL->EALE: Strongly decreased VASH1 tyrosine
FT carboxypeptidase activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31235910"
FT MUTAGEN 39..40
FT /note="IY->AA: Strongly decreased interaction with VASH1.
FT Decreased VASH1 tyrosine carboxypeptidase activity on
FT alpha-tubulin. Disrupted interaction with VASH2. Decreased
FT VASH2 tyrosine carboxypeptidase activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31171830,
FT ECO:0000269|PubMed:31235911"
FT MUTAGEN 39
FT /note="I->E: No effect on VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31235910"
FT MUTAGEN 40
FT /note="Y->F: No effect on VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 42..43
FT /note="LN->AA: Decreased interaction with VASH1. Almost
FT abolished VASH1 tyrosine carboxypeptidase activity on
FT alpha-tubulin. Strongly decreased interaction with VASH2.
FT Decreased VASH2 tyrosine carboxypeptidase activity on
FT alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31171830,
FT ECO:0000269|PubMed:31235911"
FT MUTAGEN 42
FT /note="L->E: No effect on VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31235910"
FT MUTAGEN 43
FT /note="N->A: Decreased VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 45..46
FT /note="VM->AA: Slightly decreased interaction with VASH1.
FT Decreased VASH1 tyrosine carboxypeptidase activity on
FT alpha-tubulin. No effect on interaction with VASH2. No
FT effect on VASH2 tyrosine carboxypeptidase activity on
FT alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31171830,
FT ECO:0000269|PubMed:31235911"
FT MUTAGEN 47
FT /note="T->D: Decreased VASH1 tyrosine carboxypeptidase
FT activity on alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31270470"
FT MUTAGEN 50..54
FT /note="EQQQF->AQQQA: No effect on interaction with VASH2.
FT No effect on VASH2 tyrosine carboxypeptidase activity on
FT alpha-tubulin."
FT /evidence="ECO:0000269|PubMed:31235911"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:6J4P"
FT HELIX 27..59
FT /evidence="ECO:0007829|PDB:6J4P"
SQ SEQUENCE 66 AA; 7808 MW; 9B128ABBF6ECD858 CRC64;
MDPPARKEKT KVKESVSRVE KAKQKSAQQE LKQRQRAEIY ALNRVMTELE QQQFDEFCKQ
MQPPGE
