RIMS1_RAT
ID RIMS1_RAT Reviewed; 1615 AA.
AC Q9JIR4; O35168;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 1;
DE AltName: Full=Rab-3-interacting molecule 1;
DE Short=RIM 1;
GN Name=Rims1; Synonyms=Rim1;
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] (ISOFORM 2), AND INTERACTION WITH RAB3A AND
RP RAB3C.
RC TISSUE=Brain;
RX PubMed=9252191; DOI=10.1038/41580;
RA Wang Y., Okamoto M., Schmitz F., Hofmann K., Suedhof T.C.;
RT "Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion.";
RL Nature 388:593-598(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND INTERACTION WITH RIM BINDING PROTEINS 1 AND 2.
RC TISSUE=Brain;
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 [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 INTERACTION WITH UNC13A.
RX PubMed=16704978; DOI=10.1074/jbc.m601421200;
RA Andrews-Zwilling Y.S., Kawabe H., Reim K., Varoqueaux F., Brose N.;
RT "Binding to Rab3A-interacting molecule RIM regulates the presynaptic
RT recruitment of Munc13-1 and ubMunc13-2.";
RL J. Biol. Chem. 281:19720-19731(2006).
RN [5]
RP PHOSPHORYLATION BY BRSK1.
RX PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
RA Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M.,
RA Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M.,
RA Ohtsuka T., Takai Y.;
RT "SAD: a presynaptic kinase associated with synaptic vesicles and the active
RT zone cytomatrix that regulates neurotransmitter release.";
RL Neuron 50:261-275(2006).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514; SER-592; SER-742;
RP SER-991; SER-1175; THR-1177; SER-1179; SER-1231; SER-1233; SER-1234;
RP SER-1339; SER-1600 AND SER-1603, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 [8]
RP STRUCTURE BY NMR OF 597-705 IN COMPLEX WITH ERC1, AND INTERACTION WITH
RP ERC1.
RX PubMed=16095618; DOI=10.1016/j.jmb.2005.07.047;
RA Lu J., Li H., Wang Y., Sudhof T.C., Rizo J.;
RT "Solution structure of the RIM1alpha PDZ domain in complex with an ELKS1b
RT C-terminal peptide.";
RL J. Mol. Biol. 352:455-466(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 1447-1615.
RX PubMed=17630786; DOI=10.1021/bi700698a;
RA Guan R., Dai H., Tomchick D.R., Dulubova I., Machius M., Sudhof T.C.,
RA Rizo J.;
RT "Crystal structure of the RIM1alpha C2B domain at 1.7 A resolution.";
RL Biochemistry 46:8988-8998(2007).
CC -!- FUNCTION: Rab effector involved in exocytosis. May act as scaffold
CC protein that regulates neurotransmitter release at the active zone.
CC Essential for maintaining normal probability of neurotransmitter
CC release and for regulating release during short-term synaptic
CC plasticity. Plays a role in dendrite formation by melanocytes.
CC {ECO:0000250|UniProtKB:Q86UR5, ECO:0000250|UniProtKB:Q99NE5}.
CC -!- SUBUNIT: Interacts with RAB3C, RAB10, RAB26 AND RAB37 (By similarity).
CC Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is enhanced by
CC calcium ions. Interaction with SNAP25 is weaker in the presence of
CC calcium ions. Binds RAB3A, RAB3B and RAB3D that have been activated by
CC GTP-binding. Binds UNC13A. Interacts with TSPOAP1 and RIMBP2. Interacts
CC with PPFIA3 and PPFIA4. Interacts with ERC1. {ECO:0000250,
CC ECO:0000269|PubMed:10748113, ECO:0000269|PubMed:11797009,
CC ECO:0000269|PubMed:16095618, ECO:0000269|PubMed:16704978,
CC ECO:0000269|PubMed:9252191}.
CC -!- INTERACTION:
CC Q9JIR4; O70368: Cacna1a; NbExp=2; IntAct=EBI-3507436, EBI-3507514;
CC Q9JIR4; P54282: Cacna1a; NbExp=4; IntAct=EBI-3507436, EBI-3507416;
CC Q9JIR4; O89089: Cacna1b; NbExp=2; IntAct=EBI-3507436, EBI-3507539;
CC Q9JIR4; Q811U3: Erc1; NbExp=8; IntAct=EBI-3507436, EBI-3507502;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Synapse. Presynaptic cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}. Note=Associated with plasma membranes from
CC synaptic junctions. Not detected in synaptic vesicles. Detected in
CC presynaptic nerve terminals close to the active zone. Detected in
CC synaptic ribbons of ribbon synapses of retinal photoreceptor cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Rim1B;
CC IsoId=Q9JIR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIR4-2; Sequence=VSP_008172;
CC -!- TISSUE SPECIFICITY: Highly expressed in hippocampus, brain cortex,
CC cerebellum and olfactory bulb. Detected at lower levels in midbrain,
CC hindbrain and spinal cord. Detected retina and in spinal cord motor
CC neurons. {ECO:0000269|PubMed:10748113}.
CC -!- PTM: Phosphorylated by BRSK1. {ECO:0000269|PubMed:16630837}.
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DR EMBL; AF007836; AAB66703.1; -; mRNA.
DR EMBL; AF199333; AAF81655.1; -; mRNA.
DR PIR; T03301; T03301.
DR RefSeq; NP_439894.1; NM_052829.1. [Q9JIR4-2]
DR PDB; 1ZUB; NMR; -; A=597-705.
DR PDB; 2Q3X; X-ray; 1.73 A; A/B=1447-1615.
DR PDBsum; 1ZUB; -.
DR PDBsum; 2Q3X; -.
DR AlphaFoldDB; Q9JIR4; -.
DR SMR; Q9JIR4; -.
DR BioGRID; 250003; 2.
DR CORUM; Q9JIR4; -.
DR DIP; DIP-41432N; -.
DR ELM; Q9JIR4; -.
DR IntAct; Q9JIR4; 9.
DR MINT; Q9JIR4; -.
DR STRING; 10116.ENSRNOP00000015454; -.
DR iPTMnet; Q9JIR4; -.
DR PhosphoSitePlus; Q9JIR4; -.
DR PRIDE; Q9JIR4; -.
DR GeneID; 84556; -.
DR KEGG; rno:84556; -.
DR UCSC; RGD:620000; rat. [Q9JIR4-1]
DR CTD; 22999; -.
DR RGD; 620000; Rims1.
DR eggNOG; KOG2060; Eukaryota.
DR InParanoid; Q9JIR4; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q9JIR4; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR EvolutionaryTrace; Q9JIR4; -.
DR PRO; PR:Q9JIR4; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IGI:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:RGD.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
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; ISS: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:0031632; P:positive regulation of synaptic vesicle fusion to presynaptic active zone membrane; NAS:UniProtKB.
DR GO; GO:0010808; P:positive regulation of synaptic vesicle priming; IGI:ParkinsonsUK-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; ISO:RGD.
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; 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; PF00595; PDZ; 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..1615
FT /note="Regulating synaptic membrane exocytosis protein 1"
FT /id="PRO_0000190200"
FT DOMAIN 22..205
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 619..705
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 756..879
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1461..1579
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 133..193
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UR5"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UR5"
FT VAR_SEQ 1107..1168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9252191"
FT /id="VSP_008172"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 605..616
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 628..636
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:1ZUB"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 669..673
FT /evidence="ECO:0007829|PDB:1ZUB"
FT HELIX 683..694
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 699..703
FT /evidence="ECO:0007829|PDB:1ZUB"
FT STRAND 1450..1453
FT /evidence="ECO:0007829|PDB:2Q3X"
FT TURN 1456..1458
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1464..1472
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1475..1485
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1497..1506
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1509..1515
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1526..1532
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1540..1549
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1555..1564
FT /evidence="ECO:0007829|PDB:2Q3X"
FT HELIX 1566..1568
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1575..1580
FT /evidence="ECO:0007829|PDB:2Q3X"
FT HELIX 1584..1587
FT /evidence="ECO:0007829|PDB:2Q3X"
FT STRAND 1588..1592
FT /evidence="ECO:0007829|PDB:2Q3X"
SQ SEQUENCE 1615 AA; 179655 MW; 80E76F74BF35FB7E CRC64;
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MAKPAACKTP RNAESQPHQP PLNIFRCVCV PRKPSSEEGG PERDWRLHQQ FESYKEQVRK
IGEEARRYQG EHKDDAPTCG ICHKTKFADG CGHLCSYCRT KFCARCGGRV SLRSNNEDKV
VMWVCNLCRK QQEILTKSGA WFFGSGPQQP SQDGTLSDTA TGAGSEVPRE KKARLQERSR
SQTPLSTAAV SSQDTATPGA PLHRNKGAEP SQQALGPEQK QASRSRSEPP RERKKAPGLS
EQNGKGGQKS ERKRVPKSVV QPGEGIADER ERKERRETRR LEKGRSQDYS DRPEKRDNGR
VAEDQKQRKE EEYQTRYRSD PNLARYPVKA PPEEQQMRMH ARVSRARHER RHSDVALPHT
EAAAAAPAEA TAGKRAPATA RVSPPESPRA RAAAAQPPTE HGPPPPRPAP GPAEPPEPRV
PEPLRKQGRL DPGSAVLLRK AKREKAESML RNDSLSSDQS ESVRPSPPKP HRPKRGGKRR
QMSVSSSEEE GVSTPEYTSC EDVELESESV SEKGDLDYYW LDPATWHSRE TSPISSHPVT
WQPSKEGDRL IGRVILNKRT TMPKESGALL GLKVVGGKMT DLGRLGAFIT KVKKGSLADV
VGHLRAGDEV LEWNGKPLPG ATNEEVYNII LESKSEPQVE IIVSRPIGDI PRIPESSHPP
LESSSSSFES QKMERPSISV ISPTSPGALK DAPQVLPGQL SVKLWYDKVG HQLIVNVLQA
TDLPPRVDGR PRNPYVKMYF LPDRSDKSKR RTKTVKKLLE PKWNQTFVYS HVHRRDFRER
MLEITVWDQP RVQDEESEFL GEILIELETA LLDDEPHWYK LQTHDESSLP LPQPSPFMPR
RHIHGESSSK KLQRSQRISD SDISDYEVDD GIGVVPPVGY RASARESKAT TLTVPEQQRT
THHRSRSVSP HRGDDQGRPR SRLPNVPLQR SLDEIHPTRR SRSPTRHHDA SRSPADHRSR
HVESQYSSEP DSELLMLPRA KRGRSAESLH MTSELQPSLD RARSASTNCL RPDTSLHSPE
RERHSRKSER CSIQKQSRKG TASDADRVLP PCLSRRGYAT PRATDQPVVR GKYPTRSRSS
EHSSVRTLCS MHHLAPGGSA PPSPLLLTRT HRQGSPTQSP PADTSFGSRR GRQLPQVPVR
SGSIEQASLV VEERTRQMKV KVHRFKQTTG SGSSQELDHE QYSKYNIHKD QYRSCDNASA
KSSDSDVSDV SAISRASSTS RLSSTSFMSE QSERPRGRIS SFTPKMQGRR MGTSGRAIIK
STSVSGEIYT LERNDGSQSD TAVGTVGAGG KKRRSSLSAK VVAIVSRRSR STSQLSQTES
GHKKLKSTIQ RSTETGMAAE MRKMVRQPSR ESTDGSINSY SSEGNLIFPG VRVGPDSQFS
DFLDGLGPAQ LVGRQTLATP AMGDIQIGME DKKGQLEVEV IRARSLTQKP GSKSTPAPYV
KVYLLENGAC IAKKKTRIAR KTLDPLYQQS LVFDESPQGK VLQVIVWGDY GRMDHKCFMG
VAQILLEELD LSSMVIGWYK LFPPSSLVDP TLAPLTRRAS QSSLESSSGP PCIRS
