SYTL2_MOUSE
ID SYTL2_MOUSE Reviewed; 950 AA.
AC Q99N50; B2RS48; B7ZNS4; Q8BT37; Q99J89; Q99J90; Q99N51; Q99N52; Q99N55;
AC Q99N56;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Synaptotagmin-like protein 2;
DE AltName: Full=Exophilin-4;
GN Name=Sytl2; Synonyms=Slp2;
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 [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH NRXN1.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA Fukuda M., Mikoshiba K.;
RT "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem
RT C2 proteins.";
RL Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11327731; DOI=10.1006/bbrc.2001.4803;
RA Fukuda M., Saegusa C., Mikoshiba K.;
RT "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3:
RT identification of the Slp homology domain.";
RL Biochem. Biophys. Res. Commun. 283:513-519(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 11), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH RAB27A, PROTEOLYTIC PROCESSING, AND TISSUE
RP SPECIFICITY.
RX PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M.,
RA Saegusa C., Fukuda M., Griffiths G.M.;
RT "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to
RT secretion from the immunological synapse.";
RL Traffic 9:446-457(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH RAB27A.
RX PubMed=11773082; DOI=10.1074/jbc.m112414200;
RA Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT functions as a novel Rab27A binding domain.";
RL J. Biol. Chem. 277:9212-9218(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-698; LYS-699;
RP LYS-700; LYS-705 AND LYS-706.
RX PubMed=15543135; DOI=10.1038/ncb1197;
RA Kuroda T.S., Fukuda M.;
RT "Rab27A-binding protein Slp2-a is required for peripheral melanosome
RT distribution and elongated cell shape in melanocytes.";
RL Nat. Cell Biol. 6:1195-1203(2004).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP RAB27A AND RAB27B.
RX PubMed=16716193; DOI=10.1111/j.1365-2443.2006.00964.x;
RA Saegusa C., Tanaka T., Tani S., Itohara S., Mikoshiba K., Fukuda M.;
RT "Decreased basal mucus secretion by Slp2-a-deficient gastric surface mucous
RT cells.";
RL Genes Cells 11:623-631(2006).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH RAB27A, AND TISSUE SPECIFICITY.
RX PubMed=17182843; DOI=10.1091/mbc.e06-10-0914;
RA Yu M., Kasai K., Nagashima K., Torii S., Yokota-Hashimoto H., Okamoto K.,
RA Takeuchi T., Gomi H., Izumi T.;
RT "Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through
RT unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain.";
RL Mol. Biol. Cell 18:688-696(2007).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORMS 9 AND 10).
RX PubMed=16376427; DOI=10.1016/j.molimm.2005.10.019;
RA Mascarell L., Auger R., Kanellopoulos J.M., Truffa-Bachi P.;
RT "The usage of alternative splice sites in Mus musculus synaptotagmin-like 2
RT gene is modulated by cyclosporin A and FK506 in T-lymphocytes.";
RL Mol. Immunol. 43:1846-1854(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Isoform 11 acts as a RAB27A effector protein and plays a role
CC in cytotoxic granule exocytosis in lymphocytes. Required for cytotoxic
CC granule docking at the immunologic synapse. Isoform 1 may play a role
CC in melanosome transport and vesicle trafficking. It controls melanosome
CC distribution in the cell periphery and regulates melanocyte morphology.
CC Isoform 1 acts as a positive mediator of mucus secretion by the surface
CC mucus cells of the stomach. Mediates basal mucus secretion by gastric
CC surface cells by promoting the proper granule biognesis and docking of
CC mucus granules with the apical plasma membrane.
CC {ECO:0000269|PubMed:15543135, ECO:0000269|PubMed:16716193,
CC ECO:0000269|PubMed:18266782}.
CC -!- SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by
CC GTP-binding. Interacts with RAB27B. {ECO:0000269|PubMed:11243866,
CC ECO:0000269|PubMed:11773082, ECO:0000269|PubMed:16716193,
CC ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Melanosome membrane
CC {ECO:0000269|PubMed:15543135}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15543135}. Note=Bound to melanosomes. Isoform 1 is
CC localized mainly on peripheral melanosomes but not on less mature
CC melanosomes around the nucleus. {ECO:0000269|PubMed:15543135}.
CC -!- SUBCELLULAR LOCATION: [Isoform 11]: Cell membrane
CC {ECO:0000269|PubMed:11243866, ECO:0000269|PubMed:17182843,
CC ECO:0000269|PubMed:18266782}. Note=In the pancreatic alpha cells
CC distributed in both peripheral and anterior regions. Localizes on the
CC glucagon granules in the cell periphery. {ECO:0000269|PubMed:17182843}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Slp2-a;
CC IsoId=Q99N50-1; Sequence=Displayed;
CC Name=2; Synonyms=Slp2-b;
CC IsoId=Q99N50-2; Sequence=VSP_007889;
CC Name=3; Synonyms=Slp2-a delta 2S-I;
CC IsoId=Q99N50-3; Sequence=VSP_007892;
CC Name=4; Synonyms=Slp2-a delta 2S-II;
CC IsoId=Q99N50-4; Sequence=VSP_007893;
CC Name=5; Synonyms=Slp2-a delta 2S-III;
CC IsoId=Q99N50-5; Sequence=VSP_007894;
CC Name=6; Synonyms=Slp2-c;
CC IsoId=Q99N50-6; Sequence=VSP_007890;
CC Name=7; Synonyms=Slp2-d delta 2S-IV;
CC IsoId=Q99N50-7; Sequence=VSP_007891;
CC Name=8;
CC IsoId=Q99N50-8; Sequence=VSP_007890, VSP_007894;
CC Name=9; Synonyms=Slp2-e;
CC IsoId=Q99N50-9; Sequence=Not described;
CC Name=10; Synonyms=Slp2-f;
CC IsoId=Q99N50-10; Sequence=Not described;
CC Name=11;
CC IsoId=Q99N50-11; Sequence=VSP_007893, VSP_007894;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney, testis and
CC in embryos after day 7. Detected at lower levels in skeletal muscle.
CC Expressed in pancreatic alpha cells. Isoform 6 is highly expressed in
CC brain, but not detectable in the other tissues tested. Isoform 1 is
CC expressed abundantly in the stomach and is predominantly localized at
CC the apical region of gastric-surface mucus cells. Isoform 11 is
CC expressed in cytotoxic T-lymphocytes (CTL).
CC {ECO:0000269|PubMed:11327731, ECO:0000269|PubMed:16716193,
CC ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782}.
CC -!- DOMAIN: The RabBD domain mediates interaction with RAB27A.
CC {ECO:0000250}.
CC -!- DOMAIN: The C2 1 domain mediates localization to the cell membrane.
CC {ECO:0000250}.
CC -!- PTM: Isoform 1 is highly susceptible to proteolytic degradation and is
CC stabilized by the interaction with RAB27A.
CC -!- DISRUPTION PHENOTYPE: Mice show a reduced number of mucus granules, a
CC deficiency of granule docking with the apical plasma membrane in the
CC gastric-surface mucus cells and reduction of mucus secretion by gastric
CC primary cells. {ECO:0000269|PubMed:16716193}.
CC -!- MISCELLANEOUS: [Isoform 9]: Due to intron retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: Due to intron retention. {ECO:0000305}.
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DR EMBL; AB057756; BAB41084.1; -; mRNA.
DR EMBL; AB050742; BAB32652.1; -; mRNA.
DR EMBL; AB057754; BAB41082.1; -; mRNA.
DR EMBL; AB057755; BAB41083.1; -; mRNA.
DR EMBL; AB057757; BAB41085.1; -; mRNA.
DR EMBL; AB057760; BAB41088.1; -; mRNA.
DR EMBL; AB057761; BAB41089.1; -; mRNA.
DR EMBL; AB057762; BAB41090.1; -; mRNA.
DR EMBL; AB057763; BAB41091.1; -; mRNA.
DR EMBL; AK027924; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC138714; AAI38715.1; -; mRNA.
DR EMBL; BC145398; AAI45399.1; -; mRNA.
DR CCDS; CCDS40017.1; -. [Q99N50-5]
DR CCDS; CCDS40018.1; -. [Q99N50-4]
DR CCDS; CCDS80750.1; -. [Q99N50-1]
DR CCDS; CCDS80751.1; -. [Q99N50-3]
DR RefSeq; NP_001035174.1; NM_001040085.2. [Q99N50-4]
DR RefSeq; NP_001035176.1; NM_001040087.2. [Q99N50-6]
DR RefSeq; NP_001035177.1; NM_001040088.2. [Q99N50-8]
DR RefSeq; NP_001276512.1; NM_001289583.1. [Q99N50-1]
DR RefSeq; NP_001276513.1; NM_001289584.1. [Q99N50-3]
DR RefSeq; NP_001276515.1; NM_001289586.1. [Q99N50-6]
DR RefSeq; NP_113571.2; NM_031394.3. [Q99N50-5]
DR AlphaFoldDB; Q99N50; -.
DR SMR; Q99N50; -.
DR BioGRID; 219955; 4.
DR IntAct; Q99N50; 3.
DR STRING; 10090.ENSMUSP00000102829; -.
DR iPTMnet; Q99N50; -.
DR PhosphoSitePlus; Q99N50; -.
DR EPD; Q99N50; -.
DR MaxQB; Q99N50; -.
DR PaxDb; Q99N50; -.
DR PeptideAtlas; Q99N50; -.
DR PRIDE; Q99N50; -.
DR ProteomicsDB; 254745; -. [Q99N50-1]
DR ProteomicsDB; 254746; -. [Q99N50-2]
DR ProteomicsDB; 254747; -. [Q99N50-3]
DR ProteomicsDB; 254748; -. [Q99N50-4]
DR ProteomicsDB; 254749; -. [Q99N50-5]
DR ProteomicsDB; 254750; -. [Q99N50-6]
DR ProteomicsDB; 254751; -. [Q99N50-7]
DR ProteomicsDB; 254752; -. [Q99N50-8]
DR ProteomicsDB; 254753; -. [Q99N50-11]
DR Antibodypedia; 49544; 75 antibodies from 13 providers.
DR DNASU; 83671; -.
DR Ensembl; ENSMUST00000107210; ENSMUSP00000102828; ENSMUSG00000030616. [Q99N50-5]
DR Ensembl; ENSMUST00000107211; ENSMUSP00000102829; ENSMUSG00000030616. [Q99N50-4]
DR Ensembl; ENSMUST00000190731; ENSMUSP00000139865; ENSMUSG00000030616. [Q99N50-1]
DR Ensembl; ENSMUST00000190837; ENSMUSP00000139450; ENSMUSG00000030616. [Q99N50-3]
DR GeneID; 83671; -.
DR KEGG; mmu:83671; -.
DR UCSC; uc009iha.2; mouse. [Q99N50-4]
DR UCSC; uc009ihb.2; mouse. [Q99N50-5]
DR UCSC; uc009ihc.2; mouse. [Q99N50-1]
DR UCSC; uc009ihg.2; mouse. [Q99N50-6]
DR UCSC; uc009ihh.2; mouse. [Q99N50-8]
DR UCSC; uc012fow.2; mouse. [Q99N50-3]
DR UCSC; uc029wmx.2; mouse. [Q99N50-7]
DR UCSC; uc057aig.1; mouse. [Q99N50-2]
DR CTD; 54843; -.
DR MGI; MGI:1933366; Sytl2.
DR VEuPathDB; HostDB:ENSMUSG00000030616; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155843; -.
DR HOGENOM; CLU_002711_2_0_1; -.
DR InParanoid; Q99N50; -.
DR OrthoDB; 916843at2759; -.
DR PhylomeDB; Q99N50; -.
DR BioGRID-ORCS; 83671; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Sytl2; mouse.
DR PRO; PR:Q99N50; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99N50; protein.
DR Bgee; ENSMUSG00000030616; Expressed in iris and 212 other tissues.
DR ExpressionAtlas; Q99N50; baseline and differential.
DR Genevisible; Q99N50; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:MGI.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR InterPro; IPR027006; SYTL2.
DR PANTHER; PTHR45716:SF5; PTHR45716:SF5; 2.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Exocytosis; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..950
FT /note="Synaptotagmin-like protein 2"
FT /id="PRO_0000190214"
FT DOMAIN 1..57
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 644..769
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 784..913
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..695
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11327731"
FT /id="VSP_007891"
FT VAR_SEQ 1..574
FT /note="Missing (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:11243866,
FT ECO:0000303|PubMed:11327731, ECO:0000303|PubMed:16141072"
FT /id="VSP_007890"
FT VAR_SEQ 1..487
FT /note="MIDLSFLTEEEQDAILKVLQRDAALKRAEEERVRHLPEKIKDDQQLKNMSGQ
FT WFYEAKAKRHRDKIHGADIIRASMRRKKLPAAAEQNKDTAMRAKESWVNNVNKDAVLPP
FT EIAVVEEPEDDTDPAGPSSSLVDPASSVIDMSQESTRTPAVSLPKQRKNPFNSPKLPED
FT HSLQQTKPEQSKTGKAGLFQISKEGELSESKEKSSIPDMPRQQLEKPKQTVSTEPENAS
FT HTKAPIPKARKLIYKSNDLEKDDNQSFPRQRRDSLNARGAPRGILKRNSSSSSTDSETL
FT RLNYNLDPKSKILSPGLTIHERISEKEFSLEDDSSTSSLEPLKHVRFSAVKNELPQSPR
FT PVLGQEVGEFTVLESDQLQNGTEDAGDIEEFQNHPELSHKTPLSHYQLVSSPSDSGRER
FT EQLMSSGSAPRDEIPCHSDILPTGPQCVESSSVINGQQEKSSHFTKLPSELSKSPSDEL
FT TQCGEPEPSQTADHSFRDHRQG -> MEKLNFKCMPQEPPDETIFPQKTLSIEPSKENE
FT GKNTEYFGTQVIKKACSEQEIQESIVKTSILPKVSKDTFNDRLQKLLAEATLPASQTSG
FT KEVHEQQALKVGVSENGKSFAKDEEEVTGLRESPKEPQRRNQQDCSVDKLLKESTRTPL
FT SPLQSPLEAVTTRPISPLKDDLLFEKWMKENHSPSADQREITAPFPQGVGILAGADLIQ
FT KGKHCNTEAMLQLAAEGSPPLAQLPHSFDGVSSSPADMSLSWDAQLPSENGTLPSQKEI
FT SEAIEKVVLPSKPAATDVNAVLQKLLREAGEVDAKLPEREQTAGTPSCPQRVSPLWPAP
FT DPVVPNKDFHSFCTVPDTTHEGRSHLSARMSPSAHATMSPTSTVTQYGQRLLQEVAETV
FT RETVIQPKSQYPEFRAGLEKLLKETLQTSLSKDKKDTMTISPSALTGSCEMSHQLSSEF
FT HLTEIQETVEKAEAPSVTESSFDVGLEKLLKEMSEGPCQLQASGRRDTLEKQPSQVEQA
FT GFMGEIPHHILDGPGASKMKVSCSGLESQISQCDKQLGGDEAVTGPLIDVQDNKSGFEV
FT PECSQLHEDHKIETNGTIQFVEDKGREKVITGETQASQEPGFEEAPKEMSVSRNKHSIV
FT LLETKGKAIKTREVKLVLATPYKRQEEEQGPEACSEYEFSDGNTSSNRENGRNTSS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11327731"
FT /id="VSP_007889"
FT VAR_SEQ 85..111
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11327731"
FT /id="VSP_007892"
FT VAR_SEQ 539..555
FT /note="DQKADQEPDTNECIPGI -> V (in isoform 4 and isoform
FT 11)"
FT /evidence="ECO:0000303|PubMed:11327731,
FT ECO:0000303|PubMed:18266782"
FT /id="VSP_007893"
FT VAR_SEQ 587..626
FT /note="Missing (in isoform 5, isoform 8 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:11327731,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:18266782"
FT /id="VSP_007894"
FT MUTAGEN 698
FT /note="K->Q: Loss of membrane localization; when associated
FT with Q-699; Q-700; Q-705 and Q-706."
FT /evidence="ECO:0000269|PubMed:15543135"
FT MUTAGEN 699
FT /note="K->Q: Loss of membrane localization; when associated
FT with Q-698; Q-700; Q-705 and Q-706."
FT /evidence="ECO:0000269|PubMed:15543135"
FT MUTAGEN 700
FT /note="K->Q: Loss of membrane localization; when associated
FT with Q-698; Q-699; Q-705 and Q-706."
FT /evidence="ECO:0000269|PubMed:15543135"
FT MUTAGEN 705
FT /note="K->Q: Loss of membrane localization; when associated
FT with Q-698; Q-699; Q-700 and Q-706."
FT /evidence="ECO:0000269|PubMed:15543135"
FT MUTAGEN 706
FT /note="K->Q: Loss of membrane localization; when associated
FT with Q-698; Q-699; Q-700 and Q-705."
FT /evidence="ECO:0000269|PubMed:15543135"
SQ SEQUENCE 950 AA; 106806 MW; 226B59F5A32FA4A4 CRC64;
MIDLSFLTEE EQDAILKVLQ RDAALKRAEE ERVRHLPEKI KDDQQLKNMS GQWFYEAKAK
RHRDKIHGAD IIRASMRRKK LPAAAEQNKD TAMRAKESWV NNVNKDAVLP PEIAVVEEPE
DDTDPAGPSS SLVDPASSVI DMSQESTRTP AVSLPKQRKN PFNSPKLPED HSLQQTKPEQ
SKTGKAGLFQ ISKEGELSES KEKSSIPDMP RQQLEKPKQT VSTEPENASH TKAPIPKARK
LIYKSNDLEK DDNQSFPRQR RDSLNARGAP RGILKRNSSS SSTDSETLRL NYNLDPKSKI
LSPGLTIHER ISEKEFSLED DSSTSSLEPL KHVRFSAVKN ELPQSPRPVL GQEVGEFTVL
ESDQLQNGTE DAGDIEEFQN HPELSHKTPL SHYQLVSSPS DSGREREQLM SSGSAPRDEI
PCHSDILPTG PQCVESSSVI NGQQEKSSHF TKLPSELSKS PSDELTQCGE PEPSQTADHS
FRDHRQGSEE EHSPVLKTLE RRAARKLPSK SLEDIPSDSS NQAKVDNLPE ELVRSAEDDQ
KADQEPDTNE CIPGISTVPS LPDNQFSHPD KLKRMSKSVP AFLQDESDDR ETDTASESSY
QLRRYKKSPS SLTNLSSSSG MTSLSSASGS VMSVYSGDFG NLEVKGSVQF ALDYVESLKE
LHVFVAQCKD LAAADVKKQR SDPYVKTYLL PDKGKMGKKK TLVVKKTLNP VYNEILRYKI
ERQFLKTQKL NLSVWHRDTF KRNSFLGEVE LDLETWDWDS KQNKQLKWYP LKRKTAPVAL
ETENRGEMKL ALQYVPEPSP GKKLPTTGEV HIWVKECLDL PLLRGSHLNS FVKCTILPDT
SRKSRQKTRA VGKTTNPVFN HTMVYDGFRP EDLMEACVEL TVWDHYKLTN QFLGGLRIGF
GTGKSYGTEV DWMDSTSEEV ALWEKMVNSP NTWVEATLPL RMLLIAKLSK
