RIMS2_MOUSE
ID RIMS2_MOUSE Reviewed; 1530 AA.
AC Q9EQZ7; Q8C433; Q8CCK2;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 2;
DE AltName: Full=Rab-3-interacting molecule 2;
DE Short=RIM 2;
DE AltName: Full=Rab-3-interacting protein 2;
GN Name=Rims2; Synonyms=Rab3ip2, Rim2;
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 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH RAB3A AND EPAC2.
RC TISSUE=Insulinoma;
RX PubMed=11056535; DOI=10.1038/35041046;
RA Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H.,
RA Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.;
RT "cAMP-GEFII is a direct target of cAMP in regulated exocytosis.";
RL Nat. Cell Biol. 2:805-811(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, 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 GENOMIC ORGANIZATION.
RX PubMed=12620390; DOI=10.1016/s0888-7543(02)00024-1;
RA Wang Y., Suedhof T.C.;
RT "Genomic definition of RIM proteins: evolutionary amplification of a family
RT of synaptic regulatory proteins.";
RL Genomics 81:126-137(2003).
RN [4]
RP INTERACTION WITH PCLO.
RX PubMed=12401793; DOI=10.1074/jbc.m210146200;
RA Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M., Sasaki T.,
RA Tajima N., Iwanaga T., Seino S.;
RT "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL J. Biol. Chem. 277:50497-50502(2002).
RN [5]
RP INTERACTION WITH RAB3A; RAB3B; RAB3C; RAB3D AND RAB26.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-800; SER-803;
RP SER-1515 AND SER-1518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Testis;
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: Rab effector involved in exocytosis. May act as scaffold
CC protein. Plays a role in dendrite formation by melanocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q9UQ26}.
CC -!- SUBUNIT: Interacts with TSPOAP1 and RIMBP2. Interacts with PPFIA3 and
CC PPFIA4. Interacts via its zinc finger with the first C2 domain of
CC UNC13A. Forms a complex consisting of UNC13A, RIMS2 and RAB3A (By
CC similarity). Heterodimer with PCLO. Part of a ternary complex involving
CC PCLO and EPAC2. Interacts with RAB3A and RAB3B that have been activated
CC by GTP-binding. Interacts with RAB3C, RAB3D and RAB26. {ECO:0000250,
CC ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:12401793,
CC ECO:0000269|PubMed:12578829}.
CC -!- SUBCELLULAR LOCATION: Synapse, synaptosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=RIM2-alpha;
CC IsoId=Q9EQZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=RIM2-gamma;
CC IsoId=Q9EQZ7-2; Sequence=VSP_008181, VSP_008184;
CC Name=3; Synonyms=RIM2-beta;
CC IsoId=Q9EQZ7-3; Sequence=VSP_008182, VSP_008183;
CC -!- TISSUE SPECIFICITY: Detected in testis, pituitary and an insulinoma
CC cell line. Detected at low levels in cerebellar cortex.
CC {ECO:0000269|PubMed:11056535}.
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DR EMBL; AB021131; BAB18975.1; -; mRNA.
DR EMBL; AK032619; BAC27953.1; -; mRNA.
DR EMBL; AK083172; BAC38794.1; -; mRNA.
DR CCDS; CCDS37067.1; -. [Q9EQZ7-1]
DR CCDS; CCDS88756.1; -. [Q9EQZ7-2]
DR RefSeq; NP_001243313.1; NM_001256384.1. [Q9EQZ7-2]
DR RefSeq; NP_444501.1; NM_053271.2. [Q9EQZ7-1]
DR AlphaFoldDB; Q9EQZ7; -.
DR BMRB; Q9EQZ7; -.
DR SMR; Q9EQZ7; -.
DR BioGRID; 228026; 12.
DR CORUM; Q9EQZ7; -.
DR IntAct; Q9EQZ7; 2.
DR MINT; Q9EQZ7; -.
DR STRING; 10090.ENSMUSP00000048719; -.
DR iPTMnet; Q9EQZ7; -.
DR PhosphoSitePlus; Q9EQZ7; -.
DR SwissPalm; Q9EQZ7; -.
DR MaxQB; Q9EQZ7; -.
DR PRIDE; Q9EQZ7; -.
DR ProteomicsDB; 254881; -. [Q9EQZ7-1]
DR ProteomicsDB; 254882; -. [Q9EQZ7-2]
DR ProteomicsDB; 254883; -. [Q9EQZ7-3]
DR Antibodypedia; 26403; 215 antibodies from 29 providers.
DR DNASU; 116838; -.
DR Ensembl; ENSMUST00000082054; ENSMUSP00000080711; ENSMUSG00000037386. [Q9EQZ7-1]
DR Ensembl; ENSMUST00000226410; ENSMUSP00000153868; ENSMUSG00000037386. [Q9EQZ7-2]
DR GeneID; 116838; -.
DR KEGG; mmu:116838; -.
DR UCSC; uc007vod.2; mouse. [Q9EQZ7-1]
DR UCSC; uc007voh.2; mouse. [Q9EQZ7-2]
DR CTD; 9699; -.
DR MGI; MGI:2152972; Rims2.
DR VEuPathDB; HostDB:ENSMUSG00000037386; -.
DR eggNOG; KOG2060; Eukaryota.
DR eggNOG; KOG3799; Eukaryota.
DR GeneTree; ENSGT00940000155236; -.
DR HOGENOM; CLU_001061_1_0_1; -.
DR InParanoid; Q9EQZ7; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q9EQZ7; -.
DR BioGRID-ORCS; 116838; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Rims2; mouse.
DR PRO; PR:Q9EQZ7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EQZ7; protein.
DR Bgee; ENSMUSG00000037386; Expressed in rostral migratory stream and 172 other tissues.
DR ExpressionAtlas; Q9EQZ7; baseline and differential.
DR Genevisible; Q9EQZ7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IMP:SynGO-UCL.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IGI:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IGI:ParkinsonsUK-UCL.
DR GO; GO:0016081; P:synaptic vesicle docking; IDA:SynGO.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR030631; RIM2.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; PTHR12157; 1.
DR PANTHER; PTHR12157:SF15; PTHR12157:SF15; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Differentiation; Exocytosis; Metal-binding;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; Synaptosome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1530
FT /note="Regulating synaptic membrane exocytosis protein 2"
FT /id="PRO_0000190202"
FT DOMAIN 26..194
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 677..763
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 814..937
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1376..1494
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 126..182
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ26"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS1"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS1"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS1"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008181"
FT VAR_SEQ 1..232
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008182"
FT VAR_SEQ 233..272
FT /note="PGDLSVPAVEKGRAHGLTRQDTIKNGSGVKHQIASDMPSD -> MQFETLRQ
FT VCNSVLSHFHGVFSSPPNILQNELFGQTLNNA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008183"
FT VAR_SEQ 1246..1292
FT /note="NDGSQSDTAVGALGTSGKKRRSSIGAKMVAIVGLSRKSRSASQLSQT -> M
FT GRQGLGGTGAAGRSMQRSQSRSSLSASFEALAGYFPCMNSLEEDEG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008184"
SQ SEQUENCE 1530 AA; 172863 MW; 58CF11BF7152357D CRC64;
MSAPLGPRGR PAPTPAASQP PPQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKI
KEEHKAQPTQ WFPFSGITEL VNNVLQPQQK QPNEKEPQTK LHQQFEMYKE QVKKMGEESQ
QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG GRVSLRSNKV MWVCNLCRKQ
QEILTKSGAW FYNSGSNTLQ QPDQKVPRGL RNEEAPQEKK AKLHEQPQFQ GAPGDLSVPA
VEKGRAHGLT RQDTIKNGSG VKHQIASDMP SDRKRSPSVS RDQNRRYEQS EEREDYSQYV
PSDGTMPRSP SDYADRRSQR EPQFYEEPGH LNYRDSNRRG HRHSKEYIVD DEDVESRDEY
ERQRREEEYQ ARYRSDPNLA RYPVKPQPYE EQMRIHAEVS RARHERRHSD VSLANAELED
SRISLLRMDR PSRQRSVSER RAAMENQRSY SMERTREAQG QSSYPQRTSN HSPPTPRRSP
IPLDRPDMRR ADSLRKQHHL DPSSAVRKTK REKMETMLRN DSLSSDQSES VRPPPPRPHK
SKKGGKMRQV SLSSSEEELA STPEYTSCDD VELESESVSE KGDSQKGKRK TSEQGVLSDS
NTRSERQKKR MYYGGHSLEE DLEWSEPQIK DSGVDTCSST TLNEEHSHSD KHPVTWQPSK
DGDRLIGRIL LNKRLKDGSV PRDSGAMLGL KVVGGKMTES GRLCAFITKV KKGSLADTVG
HLRPGDEVLE WNGRLLQGAT FEEVYNIILE SKPEPQVELV VSRPIGDIPR IPDSTHAQLE
SSSSSFESQK MDRPSISVTS PMSPGMLRDV PQFLSGQLSI KLWFDKVGHQ LIVTILGAKD
LPSREDGRPR NPYVKIYFLP DRSDKNKRRT KTVKKTLEPK WNQTFIYSPV HRREFRERML
EITLWDQARV REEESEFLGE ILIELETALL DDEPHWYKLQ THDVSSLPLP RPSPYLPRRQ
LHGESPTRRL QRSKRISDSE VSDYDCEDGV GVVSDYRHNG RDLQSSTLSV PEQVMSSNHC
SPSGSPHRVD VIGRTRSWSP SAPPPQRNVE QGHRGTRATG HYNTISRMDR HRVMDDHYSS
DRDRSHPRTG SVQTSPSSTP GTGRRGRQLP QLPPKGTLER SAMDIEERNR QMKLNKYKQV
AGSDPRLEQD YHSKYRSGWD PHRGADTVST KSSDSDVSDV SAVSRTSSAS RFSSTSYMSV
QSERPRGNRK ISVFTSKMQN RQMGVSGKNL TKSTSISGDM CSLEKNDGSQ SDTAVGALGT
SGKKRRSSIG AKMVAIVGLS RKSRSASQLS QTEGGGKKLR STVQRSTETG LAVEMRNWMT
RQASRESTDG SMNSYSSEGN LIFPGVRLAS DSQFSDFLDG LGPAQLVGRQ TLATPAMGDI
QVGMMDKKGQ LEVEIIRARG LVVKPGSKTL PAPYVKVYLL DNGVCIAKKK TKVARKTLEP
LYQQLLSFEE SPQGRVLQII VWGDYGRMDH KSFMGVAQIL LDELELSNMV IGWFKLFPPS
SLVDPTLAPL TRRASQSSLE SSTGPSYSRS
