STB5L_MOUSE
ID STB5L_MOUSE Reviewed; 1185 AA.
AC Q5DQR4; Q3TSM3; Q3UVG2; Q5DQR1; Q5DQR2; Q5DQR3; Q8BS52;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Syntaxin-binding protein 5-like;
DE AltName: Full=Lethal(2) giant larvae protein homolog 4;
DE AltName: Full=Tomosyn-2 {ECO:0000303|PubMed:15659226};
GN Name=Stxbp5l; Synonyms=Llgl4;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP TISSUE SPECIFICITY.
RC STRAIN=129/Ola;
RX PubMed=15659226; DOI=10.1111/j.1471-4159.2004.02890.x;
RA Groffen A.J.A., Jacobsen L., Schut D., Verhage M.;
RT "Two distinct genes drive expression of seven tomosyn isoforms in the
RT mammalian brain, sharing a conserved structure with a unique variable
RT domain.";
RL J. Neurochem. 92:554-568(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Olfactory bulb;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-567; SER-573; SER-588;
RP THR-595; SER-598; SER-792; SER-822 AND THR-1092, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, INTERACTION WITH STX1A AND STX4, TISSUE SPECIFICITY, AND VARIANT
RP LEU-937.
RX PubMed=21998599; DOI=10.1371/journal.pgen.1002323;
RA Bhatnagar S., Oler A.T., Rabaglia M.E., Stapleton D.S., Schueler K.L.,
RA Truchan N.A., Worzella S.L., Stoehr J.P., Clee S.M., Yandell B.S.,
RA Keller M.P., Thurmond D.C., Attie A.D.;
RT "Positional cloning of a type 2 diabetes quantitative trait locus; tomosyn-
RT 2, a negative regulator of insulin secretion.";
RL PLoS Genet. 7:E1002323-E1002323(2011).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-708, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [6]
RP FUNCTION, UBIQUITINATION, AND PHOSPHORYLATION AT SER-592; SER-762; SER-764;
RP SER-765; SER-770; SER-771; SER-799; SER-811; SER-819; SER-821 AND SER-822.
RX PubMed=25002582; DOI=10.1074/jbc.m114.575985;
RA Bhatnagar S., Soni M.S., Wrighton L.S., Hebert A.S., Zhou A.S., Paul P.K.,
RA Gregg T., Rabaglia M.E., Keller M.P., Coon J.J., Attie A.D.;
RT "Phosphorylation and degradation of tomosyn-2 de-represses insulin
RT secretion.";
RL J. Biol. Chem. 289:25276-25286(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24744148; DOI=10.1007/s00429-014-0766-0;
RA Geerts C.J., Plomp J.J., Koopmans B., Loos M., van der Pijl E.M.,
RA van der Valk M.A., Verhage M., Groffen A.J.;
RT "Tomosyn-2 is required for normal motor performance in mice and sustains
RT neurotransmission at motor endplates.";
RL Brain Struct. Funct. 220:1971-1982(2015).
CC -!- FUNCTION: Plays a role in vesicle trafficking and exocytosis inhibition
CC (PubMed:25002582). In pancreatic beta-cells, inhibits insulin secretion
CC probably by interacting with and regulating STX1A and STX4, key t-SNARE
CC proteins involved in the fusion of insulin granules to the plasma
CC membrane (PubMed:21998599). Also plays a role in neurotransmitter
CC release by inhibiting basal acetylcholine release from axon terminals
CC and by preventing synaptic fatigue upon repetitive stimulation
CC (PubMed:24744148). Promotes as well axonal outgrowth (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2K9, ECO:0000269|PubMed:21998599,
CC ECO:0000269|PubMed:24744148, ECO:0000269|PubMed:25002582}.
CC -!- SUBUNIT: Interacts with STX1A and STX4. {ECO:0000269|PubMed:21998599}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Note=Cytoplasmic, and associated with vesicular membranes and the
CC plasma membrane. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Tomosyn-2 isoform xb;
CC IsoId=Q5DQR4-1; Sequence=Displayed;
CC Name=2; Synonyms=Tomosyn-2 isoform m;
CC IsoId=Q5DQR4-2; Sequence=VSP_016296;
CC Name=3; Synonyms=Tomosyn-2 isoform b;
CC IsoId=Q5DQR4-3; Sequence=VSP_016295;
CC Name=4; Synonyms=Tomosyn-2 isoform s;
CC IsoId=Q5DQR4-4; Sequence=VSP_016295, VSP_016296;
CC Name=5;
CC IsoId=Q5DQR4-5; Sequence=VSP_016295, VSP_016297, VSP_016298;
CC Name=6;
CC IsoId=Q5DQR4-6; Sequence=VSP_016299;
CC Name=7;
CC IsoId=Q5DQR4-7; Sequence=VSP_016300;
CC -!- TISSUE SPECIFICITY: Detected in hippocampus and cerebellum
CC (PubMed:15659226). Expressed in pancreatic beta-cells where it
CC modulates insulin secretion (PubMed:21998599).
CC {ECO:0000269|PubMed:15659226, ECO:0000269|PubMed:21998599}.
CC -!- PTM: Phosphorylated, leading to STXBP5L increased turnover and
CC subsequent de-repression of insulin secretion (PubMed:25002582).
CC Phosphorylated on serine residues in response to glucose or phorbol
CC esters (PubMed:25002582). {ECO:0000269|PubMed:25002582}.
CC -!- PTM: Ubiquitinated by the E3 ligase SYVN1, leading to STXBP5L
CC proteasomal degradation. {ECO:0000269|PubMed:25002582}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate and show normal body weight development. However, they display
CC reduced sensorimotor gating and impaired motor performance.
CC {ECO:0000269|PubMed:24744148}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL 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; AY542354; AAT68171.1; -; Genomic_DNA.
DR EMBL; AY542328; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542329; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542331; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542330; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542332; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542334; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542336; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542338; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542340; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542349; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542348; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542347; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542346; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542345; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542344; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542343; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542342; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542341; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542353; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542352; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542351; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542350; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542339; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542337; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542335; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542333; AAT68171.1; JOINED; Genomic_DNA.
DR EMBL; AY542354; AAT68172.1; -; Genomic_DNA.
DR EMBL; AY542328; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542329; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542330; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542332; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542335; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542334; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542333; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542331; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542336; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542345; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542344; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542343; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542342; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542341; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542340; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542339; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542338; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542337; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542353; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542352; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542351; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542350; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542349; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542347; AAT68172.1; JOINED; Genomic_DNA.
DR EMBL; AY542354; AAT68173.1; -; Genomic_DNA.
DR EMBL; AY542328; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542329; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542331; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542332; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542330; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542333; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542335; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542337; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542340; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542349; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542348; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542347; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542345; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542338; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542344; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542343; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542342; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542341; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542353; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542352; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542351; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542350; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542339; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542336; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542334; AAT68173.1; JOINED; Genomic_DNA.
DR EMBL; AY542354; AAT68174.1; -; Genomic_DNA.
DR EMBL; AY542329; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542330; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542328; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542331; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542333; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542335; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542337; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542346; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542345; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542344; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542343; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542342; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542341; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542340; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542339; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542338; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542353; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542352; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542351; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542350; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542349; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542347; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542336; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542334; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542332; AAT68174.1; JOINED; Genomic_DNA.
DR EMBL; AY542324; AAT68175.1; -; mRNA.
DR EMBL; AY542325; AAT68176.1; -; mRNA.
DR EMBL; AY542326; AAT68177.1; -; mRNA.
DR EMBL; AY542327; AAT68178.1; -; mRNA.
DR EMBL; AK035159; BAC28964.1; -; mRNA.
DR EMBL; AK137325; BAE23307.1; -; mRNA.
DR EMBL; AK161955; BAE36652.1; -; mRNA.
DR CCDS; CCDS28159.2; -. [Q5DQR4-1]
DR CCDS; CCDS49846.1; -. [Q5DQR4-4]
DR CCDS; CCDS49847.1; -. [Q5DQR4-3]
DR CCDS; CCDS49848.1; -. [Q5DQR4-2]
DR RefSeq; NP_001108083.1; NM_001114611.1. [Q5DQR4-4]
DR RefSeq; NP_001108084.1; NM_001114612.1. [Q5DQR4-3]
DR RefSeq; NP_001108085.1; NM_001114613.1. [Q5DQR4-2]
DR RefSeq; NP_766028.2; NM_172440.3. [Q5DQR4-1]
DR AlphaFoldDB; Q5DQR4; -.
DR SMR; Q5DQR4; -.
DR IntAct; Q5DQR4; 1.
DR STRING; 10090.ENSMUSP00000110435; -.
DR iPTMnet; Q5DQR4; -.
DR PhosphoSitePlus; Q5DQR4; -.
DR SwissPalm; Q5DQR4; -.
DR MaxQB; Q5DQR4; -.
DR PaxDb; Q5DQR4; -.
DR PeptideAtlas; Q5DQR4; -.
DR PRIDE; Q5DQR4; -.
DR ProteomicsDB; 257480; -. [Q5DQR4-1]
DR ProteomicsDB; 257481; -. [Q5DQR4-2]
DR ProteomicsDB; 257482; -. [Q5DQR4-3]
DR ProteomicsDB; 257483; -. [Q5DQR4-4]
DR ProteomicsDB; 257484; -. [Q5DQR4-5]
DR ProteomicsDB; 257485; -. [Q5DQR4-6]
DR ProteomicsDB; 257486; -. [Q5DQR4-7]
DR Antibodypedia; 32817; 5 antibodies from 4 providers.
DR DNASU; 207227; -.
DR Ensembl; ENSMUST00000114775; ENSMUSP00000110423; ENSMUSG00000022829. [Q5DQR4-6]
DR Ensembl; ENSMUST00000114780; ENSMUSP00000110428; ENSMUSG00000022829. [Q5DQR4-4]
DR Ensembl; ENSMUST00000114781; ENSMUSP00000110429; ENSMUSG00000022829. [Q5DQR4-2]
DR Ensembl; ENSMUST00000114782; ENSMUSP00000110430; ENSMUSG00000022829. [Q5DQR4-3]
DR Ensembl; ENSMUST00000114787; ENSMUSP00000110435; ENSMUSG00000022829. [Q5DQR4-1]
DR GeneID; 207227; -.
DR KEGG; mmu:207227; -.
DR UCSC; uc007zds.2; mouse. [Q5DQR4-1]
DR UCSC; uc007zdt.2; mouse. [Q5DQR4-2]
DR UCSC; uc007zdu.2; mouse. [Q5DQR4-3]
DR UCSC; uc007zdv.2; mouse. [Q5DQR4-4]
DR UCSC; uc007zdw.2; mouse. [Q5DQR4-5]
DR UCSC; uc007zdx.2; mouse. [Q5DQR4-6]
DR UCSC; uc007zdy.2; mouse. [Q5DQR4-7]
DR CTD; 9515; -.
DR MGI; MGI:2443815; Stxbp5l.
DR VEuPathDB; HostDB:ENSMUSG00000022829; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR HOGENOM; CLU_002808_0_0_1; -.
DR InParanoid; Q5DQR4; -.
DR OMA; PNXFPIF; -.
DR OrthoDB; 84844at2759; -.
DR PhylomeDB; Q5DQR4; -.
DR TreeFam; TF314585; -.
DR BioGRID-ORCS; 207227; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Stxbp5l; mouse.
DR PRO; PR:Q5DQR4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5DQR4; protein.
DR Bgee; ENSMUSG00000022829; Expressed in animal zygote and 44 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR Pfam; PF08366; LLGL; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50892; V_SNARE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Exocytosis; Membrane; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..1185
FT /note="Syntaxin-binding protein 5-like"
FT /id="PRO_0000051248"
FT REPEAT 73..106
FT /note="WD 1"
FT REPEAT 113..152
FT /note="WD 2"
FT REPEAT 157..193
FT /note="WD 3"
FT REPEAT 212..246
FT /note="WD 4"
FT REPEAT 252..284
FT /note="WD 5"
FT REPEAT 306..348
FT /note="WD 6"
FT REPEAT 356..390
FT /note="WD 7"
FT REPEAT 412..489
FT /note="WD 8"
FT REPEAT 517..628
FT /note="WD 9"
FT REPEAT 642..704
FT /note="WD 10"
FT REPEAT 831..888
FT /note="WD 11"
FT REPEAT 897..968
FT /note="WD 12"
FT REPEAT 973..1017
FT /note="WD 13"
FT REPEAT 1031..1054
FT /note="WD 14"
FT DOMAIN 1120..1180
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 15..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K9"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 708
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25002582,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1092
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 157..1185
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016300"
FT VAR_SEQ 467..1185
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016299"
FT VAR_SEQ 703..727
FT /note="DNFCMRGLSNFYPDLTKRIRTSYQS -> G (in isoform 3,
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15659226,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016295"
FT VAR_SEQ 749..805
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15659226"
FT /id="VSP_016296"
FT VAR_SEQ 1006..1025
FT /note="SLPSLRPMLDVNYLPLTDMR -> RYMVYLLLTDNHNNASKVKW (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016297"
FT VAR_SEQ 1026..1185
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016298"
FT VARIANT 937
FT /note="S -> L (results in attenuation of insulin secretion;
FT increased protein stability)"
FT /evidence="ECO:0000269|PubMed:21998599"
SQ SEQUENCE 1185 AA; 131844 MW; 0F797A5CF20E05DC CRC64;
MKKFNFRKVL DGLTASSPGS GSSSGSNSGG AGSGSVHPGG TAGLPREEIQ ESLTSDYFQI
CKTVRHGFPY QPTALAFDPV QKILAIGTRT GAIRILGRPG VDCYCQHESG AAVLQLQFLI
NEGALVSASS DDTLHLWNLR QKRPAILHSL KFNRERITYC HLPFQSKWLY VGTERGNTHI
VNIESFILSG YVIMWNKAIE LSTKTHPGPV VHLSDSPRDE GKLLIGYENG TVVFWDLKSK
RAELRVYYDE AIHSIDWHHE GKQFMCSHSD GSLTLWNLKS PSRPFQTTVP HGKSQREGRK
SESCKPILKV EYKTCRNSEP FIIFSGGLSY DKACRRPSLT IMHGKAITVL EMDHPIVEFL
TLCETPYPNE FQEPYAVAVL LEKDLIVVDL TQTNFPIFEN PYPMDIHESP VTCTAYFADC
PPDLILVLYS IGVKHKKQGY SNKEWPVSGG AWNLGAQTYP EIIITGHADG TIKFWDASAM
TLQMLYKLKT SKVFEKQKAG EGKQTCELVE EDPFAVQMIY WCPESRIFCV SGVSAYVIIY
KFSRHEVTTE IVSLEVRLQC DVEDIITPEP ETSPPFPDLS SQLPPSRSLS GSTNTVSSEG
VTKDSIPCLS VKTRPVRMPP GYQADLVIQL VWVDGEPPQQ ITSLSISSAY GIVAFGNCTG
LVVVDFIQKT VLLSMGTIDL YRSSDLYQRQ PRSPRKNRQF IADNFCMRGL SNFYPDLTKR
IRTSYQSLTE LNDSPVPLEL ERCKSPTSDH VNGHCTSPTS QSCSSGKRLS SADVSKVNRW
GPGRPPFRKA QSAACMEISL PVTTEETREN SYNRSRSSSI SSIDKDSKEA ITALYFMESF
ARKNDSTVSP CLFVGTSLGM VVLISLNLPS SDEQRFTEPV VVLPSGTFLS LKGAVLTFSC
MDRTGSLMQP PYEVWRDPNN TDENEKTWKR KLVMNYSSSS QEMGDHQYTI ICSEKQAKVF
SLPSQTCLYV HNITETSFIL QADVVVMCNS ACLACFCANG HIMIMSLPSL RPMLDVNYLP
LTDMRIARTF CFTNEGQALY LVSPTEIQRL TYSQEMCDNI QDMLGDLFTP IETPEAQNRG
FLKGLFGGSG QTFDREELFG EASAGKASRS LAQHIPGPGS IEGMKGAAGG VMGELTRARI
ALDERGQRLG ELEEKTAGMM TSAEAFSKHA HELMLKYKDK KWYQF
