RIMS2_RAT
ID RIMS2_RAT Reviewed; 1555 AA.
AC Q9JIS1; Q8CIX2; Q9JHJ6; Q9JIR2; Q9JIR5; Q9JIR6; Q9JIR7; Q9JIR8; Q9JIR9;
AC Q9JIS0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 2;
DE AltName: Full=Rab-3-interacting molecule 2;
DE Short=RIM 2;
GN Name=Rims2; Synonyms=Rim2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 8; 9 AND 10), TISSUE
RP SPECIFICITY, AND INTERACTION WITH RAB3A; RAB3B; RIM BINDING PROTEINS 1 AND
RP 2.
RX PubMed=10748113; DOI=10.1074/jbc.m909008199;
RA Wang Y., Sugita S., Suedhof T.C.;
RT "The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3
RT and a new class of Src homology 3 domain proteins.";
RL J. Biol. Chem. 275:20033-20044(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND 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 [3]
RP INTERACTION WITH PPFIA3 AND PPFIA4.
RC TISSUE=Brain;
RX PubMed=11797009; DOI=10.1038/415321a;
RA Schoch S., Castillo P.E., Jo T., Mukherjee K., Geppert M., Wang Y.,
RA Schmitz F., Malenka R.C., Suedhof T.C.;
RT "RIM1alpha forms a protein scaffold for regulating neurotransmitter release
RT at the active zone.";
RL Nature 415:321-326(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106; SER-1200; SER-1276;
RP SER-1540 AND SER-1543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 83-142 IN COMPLEX WITH UNC13A.
RX PubMed=16732694; DOI=10.1371/journal.pbio.0040192;
RA Lu J., Machius M., Dulubova I., Dai H., Suedhof T.C., Tomchick D.R.,
RA Rizo J.;
RT "Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer
RT switch.";
RL PLoS Biol. 4:1159-1172(2006).
RN [7]
RP STRUCTURE BY NMR OF 83-142, AND INTERACTION WITH UNC13A.
RX PubMed=16052212; DOI=10.1038/sj.emboj.7600753;
RA Dulubova I., Lou X., Lu J., Huryeva I., Alam A., Schneggenburger R.,
RA Suedhof T.C., Rizo J.;
RT "A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?";
RL EMBO J. 24:2839-2850(2005).
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: Heterodimer with PCLO. Part of a ternary complex involving
CC PCLO and EPAC2. Interacts with RAB3C, RAB3D and RAB26 (By similarity).
CC Binds RAB3A and RAB3B that have been activated by GTP-binding.
CC Interacts with TSPOAP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4.
CC Interacts via its zinc finger with the first C2 domain of UNC13A. Forms
CC a complex consisting of UNC13A, RIMS2 and RAB3A. {ECO:0000250,
CC ECO:0000269|PubMed:10748113, ECO:0000269|PubMed:11797009,
CC ECO:0000269|PubMed:16052212, ECO:0000269|PubMed:16732694}.
CC -!- INTERACTION:
CC Q9JIS1; Q62768: Unc13a; NbExp=4; IntAct=EBI-6972631, EBI-15584670;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=RIM2-alpha;
CC IsoId=Q9JIS1-1; Sequence=Displayed;
CC Name=2; Synonyms=RIM2-2B;
CC IsoId=Q9JIS1-2; Sequence=VSP_008186, VSP_008187, VSP_008189;
CC Name=3; Synonyms=RIM2-4C;
CC IsoId=Q9JIS1-3; Sequence=VSP_008187, VSP_008188, VSP_008189;
CC Name=4; Synonyms=RIM2-5C, RIM2-2A, RIM2-3B, RIM2-4A;
CC IsoId=Q9JIS1-4; Sequence=VSP_008187, VSP_008189;
CC Name=5; Synonyms=RIM2-3A;
CC IsoId=Q9JIS1-5; Sequence=VSP_008189;
CC Name=6; Synonyms=RIM2-4B;
CC IsoId=Q9JIS1-6; Sequence=VSP_008187, VSP_008191, VSP_008189;
CC Name=7; Synonyms=RIM2-beta, RIM2beta;
CC IsoId=Q9JIS1-7; Sequence=VSP_008185;
CC Name=8; Synonyms=RIM2-5B;
CC IsoId=Q9JIS1-8; Sequence=VSP_008187, VSP_008190;
CC Name=9; Synonyms=RIM2-5A;
CC IsoId=Q9JIS1-9; Sequence=VSP_008187;
CC Name=10; Synonyms=RIM2-gamma, NIM2;
CC IsoId=Q9JIS1-10; Sequence=VSP_008192, VSP_008193;
CC -!- TISSUE SPECIFICITY: Highly expressed in hippocampus, brain cortex,
CC cerebellum and olfactory bulb. Detected at intermediate levels in
CC midbrain, hindbrain and spinal cord, and at low levels in testis.
CC {ECO:0000269|PubMed:10748113}.
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; AF199322; AAF81644.1; -; mRNA.
DR EMBL; AF199323; AAF81645.1; -; mRNA.
DR EMBL; AF199324; AAF81646.1; -; mRNA.
DR EMBL; AF199325; AAF81647.1; -; mRNA.
DR EMBL; AF199326; AAF81648.1; -; mRNA.
DR EMBL; AF199327; AAF81649.1; -; mRNA.
DR EMBL; AF199328; AAF81650.1; -; mRNA.
DR EMBL; AF199329; AAF81651.1; -; mRNA.
DR EMBL; AF199330; AAF81652.1; -; mRNA.
DR EMBL; AF199331; AAF81653.1; -; mRNA.
DR EMBL; AF199332; AAF81654.1; -; mRNA.
DR EMBL; AF199335; AAF81657.1; -; mRNA.
DR EMBL; AF548738; AAN59930.1; -; mRNA.
DR RefSeq; NP_446397.1; NM_053945.2. [Q9JIS1-1]
DR RefSeq; NP_665888.1; NM_145881.2. [Q9JIS1-10]
DR PDB; 2A20; NMR; -; A=83-142.
DR PDB; 2BWQ; X-ray; 1.41 A; A=725-869.
DR PDB; 2CJS; X-ray; 1.78 A; C=83-142.
DR PDBsum; 2A20; -.
DR PDBsum; 2BWQ; -.
DR PDBsum; 2CJS; -.
DR AlphaFoldDB; Q9JIS1; -.
DR BMRB; Q9JIS1; -.
DR SMR; Q9JIS1; -.
DR BioGRID; 250611; 4.
DR CORUM; Q9JIS1; -.
DR DIP; DIP-29192N; -.
DR IntAct; Q9JIS1; 2.
DR MINT; Q9JIS1; -.
DR STRING; 10116.ENSRNOP00000045165; -.
DR iPTMnet; Q9JIS1; -.
DR PhosphoSitePlus; Q9JIS1; -.
DR PaxDb; Q9JIS1; -.
DR PRIDE; Q9JIS1; -.
DR Ensembl; ENSRNOT00000006393; ENSRNOP00000006393; ENSRNOG00000004201. [Q9JIS1-10]
DR GeneID; 116839; -.
DR KEGG; rno:116839; -.
DR CTD; 9699; -.
DR RGD; 620001; Rims2.
DR VEuPathDB; HostDB:ENSRNOG00000004201; -.
DR eggNOG; KOG2060; Eukaryota.
DR eggNOG; KOG3799; Eukaryota.
DR GeneTree; ENSGT00940000155236; -.
DR HOGENOM; CLU_071205_0_0_1; -.
DR InParanoid; Q9JIS1; -.
DR OrthoDB; 109268at2759; -.
DR EvolutionaryTrace; Q9JIS1; -.
DR PRO; PR:Q9JIS1; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004201; Expressed in frontal cortex and 16 other tissues.
DR ExpressionAtlas; Q9JIS1; baseline and differential.
DR Genevisible; Q9JIS1; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; TAS:RGD.
DR GO; GO:0030073; P:insulin secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
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; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; PTHR12157; 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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Differentiation; Exocytosis; Membrane; Metal-binding;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1555
FT /note="Regulating synaptic membrane exocytosis protein 2"
FT /id="PRO_0000190203"
FT DOMAIN 26..154
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 590..676
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 743..866
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1401..1519
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 86..142
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1332
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 167..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ26"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ26"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ7"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ7"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..1270
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008192"
FT VAR_SEQ 1..232
FT /note="MSAPLGPRGRPAPTPAASQPPPQPEMPDLSHLTEEERKIIQAVMDRQKKEEE
FT KEQSVLKKLHQQFEMYKEQVKKMGEESQQQQEQKGDAPTCGICHKTKFADGCGHNCSYC
FT QTKFCARCGGRVSLRSNKVMWVCNLCRKQQEILTKSGAWFYNSGSNTPQQPDQKALRGL
FT RSEEAPQEKKAKLHEQTQFQGPPGDSSVPAVERGRAHGLTRQDSIKNGSGMKHQIASDM
FT PSD -> MQFETLRQVCNSVLSHFHGVFSSPPNILQNELFGQTLNNA (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:12620390"
FT /id="VSP_008185"
FT VAR_SEQ 544..564
FT /note="MEYSWLEHASWHSSEASPMSL -> SQKGKRKTSEQAVWSDSNTRSERQKKV
FT MYSGGHSLDEDLEWSEPQTKDSGVDTCSSTTLNEERSHSDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008186"
FT VAR_SEQ 733..748
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 6, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008187"
FT VAR_SEQ 1013..1034
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008188"
FT VAR_SEQ 1035..1094
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008191"
FT VAR_SEQ 1132..1318
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008189"
FT VAR_SEQ 1132..1146
FT /note="MITEDMDSTRKRNSG -> S (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008190"
FT VAR_SEQ 1271..1317
FT /note="NDGSQSDTAVGALGTSGKKRRSSIGAKMVAIVGLSRKSRSASQLSQT -> M
FT GRQGLGGTGAAGRSMQRSQSRSSLSASFEALAGYFPCMNSLEEDEG (in isoform
FT 10)"
FT /evidence="ECO:0000303|PubMed:10748113"
FT /id="VSP_008193"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2CJS"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2CJS"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2CJS"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2CJS"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2CJS"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2CJS"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:2CJS"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 749..754
FT /evidence="ECO:0007829|PDB:2BWQ"
FT TURN 755..758
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 759..769
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 781..790
FT /evidence="ECO:0007829|PDB:2BWQ"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 809..816
FT /evidence="ECO:0007829|PDB:2BWQ"
FT HELIX 821..826
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 828..835
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 845..853
FT /evidence="ECO:0007829|PDB:2BWQ"
FT HELIX 854..856
FT /evidence="ECO:0007829|PDB:2BWQ"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:2BWQ"
SQ SEQUENCE 1555 AA; 175913 MW; D76967BB36D9704E CRC64;
MSAPLGPRGR PAPTPAASQP PPQPEMPDLS HLTEEERKII QAVMDRQKKE EEKEQSVLKK
LHQQFEMYKE QVKKMGEESQ QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG
GRVSLRSNKV MWVCNLCRKQ QEILTKSGAW FYNSGSNTPQ QPDQKALRGL RSEEAPQEKK
AKLHEQTQFQ GPPGDSSVPA VERGRAHGLT RQDSIKNGSG MKHQIASDMP SDRKRSPSVS
RDQNRRYDQS EEREEYSQYV PSDSTMPRSP SDYADRRSQR EPQFYEEPDH LNYRDSNRRG
HRHSKEYIVD DEDVESRDEY ERQRREEEYQ ARYRSDPNLA RYPVKPQPYE EQMRIHAEVS
RARHERRHSD VSLANAELED SRISLLRMDR PSRQRSVSER RAAMENQRSY SMERTREAQG
QSSYPQRTTN HSPPTPRRSP IPLDRPELRR ADSLRKQHHL DPSSAVRKTK REKMETMLRN
DSLSSDQSES VRPPPPRPHK SKKGGKMRQV SLSSSEEELA STPEYTSCDD VEIESESVGE
KGDMEYSWLE HASWHSSEAS PMSLHPVTWQ PSKDGDRLIG RILLNKRLKD GSVPRDSGAM
LGLKVVGGKM TESGRLCAFI TKVKKGSLAD TVGHLRPGDE VLEWNGRLLQ GATFEEVYNI
ILESKPEPQV ELVVSRPIGD MPRIPDSTHA QLESSSSSFE SQKMDRPSIS VTSPMSPGML
RDVPQFLSGQ LSSQSLSRRT TPFVPRVQIK LWFDKVGHQL IVTILGAKDL PSREDGRPRN
PYVKIYFLPD RSDKNKRRTK TVKKTLEPKW NQTFIYSPVH RREFRERMLE ITLWDQARVR
EEESEFLGEI LIELETALLD DEPHWYKLQT HDVSSLPLPH PSPYMPRRQL HGESPTRRLQ
RSKRISDSEV SDYDCEDGVG VVSDYRHDGR DLQSSTLSVP EQVMSSNHCS PSGSPHRVDV
IGRTRSWSPS VPPPQRNVEQ GLRGTRATGH YNTISRMDRH RVMDDHYSSE RDSHFLTLPR
SRHRQTSEHH HRDGRDCEAA DRQPYHRSRS TEQRPLLERT TTRSRSSERA DTNLMRSMPS
LMTGRSAPPS PALSRSHPRT GSVQTSPSST PVTGRRGRQL PQLPPKGTLE RMITEDMDST
RKRNSGAMDI EERNRQMKLN KYKQVAGSDP RLEQDYHSKY RSGWDPHRGA DTVSTKSSDS
DVSDVSAVSR TSSASRFSST SYMSVQSERP RGNRKISVFT SKMQSRQMGV SGKSMAKSTS
ISGDMCSLEK NDGSQSDTAV GALGTSGKKR RSSIGAKMVA IVGLSRKSRS ASQLSQTEGG
GKKLRSTVQR STETGLAVEM RNWMTRQASR ESTDGSMNSY SSEGNLIFPG VRLASDSQFS
DFLDGLGPAQ LVGRQTLATP AMGDIQVGMM DKKGQLEVEI IRARGLVVKP GSKTLPAPYV
KVYLLDNGVC IAKKKTKVAR KTLEPLYQQL LSFEESPQGK VLQIIVWGDY GRMDHKSFMG
VAQILLDELE LSNMVIGWFK LFPPSSLVDP TLAPLTRRAS QSSLESSTGP SYSRS
