GRIP1_RAT
ID GRIP1_RAT Reviewed; 1112 AA.
AC P97879;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glutamate receptor-interacting protein 1;
DE Short=GRIP-1;
DE AltName: Full=AMPA receptor-interacting protein GRIP1;
GN Name=Grip1;
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 1), INTERACTION WITH GRIA2 AND GRIA3,
RP TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Hippocampus;
RX PubMed=9069286; DOI=10.1038/386279a0;
RA Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.;
RT "GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA
RT receptors.";
RL Nature 386:279-284(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GRIA2 AND GRIA3.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=15226318; DOI=10.1074/jbc.m405786200;
RA Charych E.I., Yu W., Li R., Serwanski D.R., Miralles C.P., Li X.,
RA Yang B.Y., Pinal N., Walikonis R., De Blas A.L.;
RT "A four PDZ domain-containing splice variant form of GRIP1 is localized in
RT GABAergic and glutamatergic synapses in the brain.";
RL J. Biol. Chem. 279:38978-38990(2004).
RN [3]
RP SUBUNIT, INTERACTION WITH GRIA2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10436050; DOI=10.1523/jneurosci.19-16-06930.1999;
RA Dong H., Zhang P., Song I., Petralia R.S., Liao D., Huganir R.L.;
RT "Characterization of the glutamate receptor-interacting proteins GRIP1 and
RT GRIP2.";
RL J. Neurosci. 19:6930-6941(1999).
RN [4]
RP INTERACTION WITH GRIPAP1.
RX PubMed=10896157; DOI=10.1016/s0896-6273(00)81198-8;
RA Ye B., Liao D., Zhang X., Zhang P., Dong H., Huganir R.L.;
RT "GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP
RT complex.";
RL Neuron 26:603-617(2000).
RN [5]
RP INTERACTION WITH PPFIA1; PPFIA4; PTPRF AND LIPRINS-ALPHA.
RX PubMed=11931740; DOI=10.1016/s0896-6273(02)00640-2;
RA Wyszynski M., Kim E., Dunah A.W., Passafaro M., Valtschanoff J.G.,
RA Serra-Pages C., Streuli M., Weinberg R.J., Sheng M.;
RT "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA
RT receptor targeting.";
RL Neuron 34:39-52(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12115684; DOI=10.1002/cne.10280;
RA Gabriel R., de Souza S., Ziff E.B., Witkovsky P.;
RT "Association of the AMPA receptor-related postsynaptic density proteins
RT GRIP and ABP with subsets of glutamate-sensitive neurons in the rat
RT retina.";
RL J. Comp. Neurol. 449:129-140(2002).
RN [7]
RP INTERACTION WITH NSG1, COMPLEX FORMATION WITH NSG1; GRIA2 AND STX12, AND
RP FUNCTION.
RX PubMed=16037816; DOI=10.1038/sj.emboj.7600755;
RA Steiner P., Alberi S., Kulangara K., Yersin A., Sarria J.C., Regulier E.,
RA Kasas S., Dietler G., Muller D., Catsicas S., Hirling H.;
RT "Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and
RT recycling of the glutamate receptor subunit GluR2.";
RL EMBO J. 24:2873-2884(2005).
RN [8]
RP INTERACTION WITH ATAD1 AND GRIA2.
RX PubMed=21496646; DOI=10.1016/j.cell.2011.03.016;
RA Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H.,
RA Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M.,
RA Dawson V.L.;
RT "The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic
RT plasticity and behavior.";
RL Cell 145:284-299(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
RP STRUCTURE BY NMR OF 980-1070, AND INTERACTION WITH GRASP1.
RX PubMed=12196542; DOI=10.1074/jbc.m207206200;
RA Feng W., Fan J.-S., Jiang M., Shi Y.-W., Zhang M.;
RT "PDZ7 of glutamate receptor interacting protein binds to its target via a
RT novel hydrophobic surface area.";
RL J. Biol. Chem. 277:41140-41146(2002).
RN [11]
RP INTERACTION WITH CSPG4, AND DOMAIN.
RX PubMed=12458226; DOI=10.1074/jbc.m210010200;
RA Stegmueller J., Werner H., Nave K.-A., Trotter J.;
RT "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-
RT isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor
RT interaction protein (GRIP) in glial progenitor cells. Implications for
RT glial-neuronal signaling.";
RL J. Biol. Chem. 278:3590-3598(2003).
RN [12]
RP INTERACTION WITH FRAS1.
RX PubMed=14730302; DOI=10.1038/ng1292;
RA Takamiya K., Kostourou V., Adams S., Jadeja S., Chalepakis G.,
RA Scambler P.J., Huganir R.L., Adams R.H.;
RT "A direct functional link between the multi-PDZ domain protein GRIP1 and
RT the Fraser syndrome protein Fras1.";
RL Nat. Genet. 36:172-177(2004).
CC -!- FUNCTION: May play a role as a localized scaffold for the assembly of a
CC multiprotein signaling complex and as mediator of the trafficking of
CC its binding partners at specific subcellular location in neurons
CC (PubMed:9069286). Through complex formation with NSG1, GRIA2 and STX12
CC controls the intracellular fate of AMPAR and the endosomal sorting of
CC the GRIA2 subunit toward recycling and membrane targeting
CC (PubMed:16037816). {ECO:0000269|PubMed:16037816,
CC ECO:0000269|PubMed:9069286}.
CC -!- SUBUNIT: Interacts with EFNB1, EPHA7, EPHB2, EFNB3, KIF5A, KIF5C, KIF5B
CC and the C-terminal tail of PRLHR. Forms a ternary complex with GRIA2
CC and CSPG4 (By similarity). Can form homomultimers or heteromultimers
CC with GRIP2. Interacts with GRIA2, GRIA3, GRIPAP1/GRASP1, PPFIA1,
CC PPFIA4, FRAS1, PLCD4, PTPRF and liprins-alpha. Interacts with ATAD1 in
CC an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts
CC binding to ATAD1 and to GRIA2 and leads to AMPAR complex disassembly.
CC Interacts with SLC30A9 (By similarity). Interacts with BUD23 (By
CC similarity). Forms a complex with NSG1, GRIA2 and STX12; controls the
CC intracellular fate of AMPAR and the endosomal sorting of the GRIA2
CC subunit toward recycling and membrane targeting (PubMed:16037816).
CC Interacts with NSG1 (PubMed:16037816). {ECO:0000250,
CC ECO:0000269|PubMed:16037816}.
CC -!- INTERACTION:
CC P97879; Q8CGU4: Agap2; NbExp=4; IntAct=EBI-936113, EBI-4409108;
CC P97879; P19491: Gria2; NbExp=15; IntAct=EBI-936113, EBI-77718;
CC P97879; P19492: Gria3; NbExp=3; IntAct=EBI-936113, EBI-77764;
CC P97879; P19493: Gria4; NbExp=3; IntAct=EBI-936113, EBI-7761834;
CC P97879; Q9WTW1-3: Grip2; NbExp=3; IntAct=EBI-936113, EBI-936068;
CC P97879; P35400: Grm7; NbExp=3; IntAct=EBI-936113, EBI-6936416;
CC P97879; Q91Z79: Ppfia3; NbExp=3; IntAct=EBI-936113, EBI-8276993;
CC P97879; Q91Z80: Ppfia4; NbExp=7; IntAct=EBI-936113, EBI-8276907;
CC P97879; Q9WUL3: RPTPK; NbExp=2; IntAct=EBI-936113, EBI-8277319;
CC P97879; Q13136: PPFIA1; Xeno; NbExp=4; IntAct=EBI-936113, EBI-745426;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10436050}. Perikaryon
CC {ECO:0000269|PubMed:10436050}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10436050}. Cytoplasm {ECO:0000269|PubMed:10436050}.
CC Endomembrane system; Peripheral membrane protein. Postsynaptic cell
CC membrane {ECO:0000269|PubMed:10436050}. Postsynaptic density
CC {ECO:0000269|PubMed:10436050, ECO:0000269|PubMed:15226318}. Endoplasmic
CC reticulum membrane {ECO:0000305|PubMed:10436050}; Peripheral membrane
CC protein {ECO:0000305}. Note=Membrane-associated with vesicles, peri-
CC Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic
CC plasma membrane and postsynaptic densities.
CC {ECO:0000269|PubMed:10436050}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97879-1; Sequence=Displayed;
CC Name=2; Synonyms=GRIP1c4-7;
CC IsoId=P97879-2; Sequence=VSP_009751, VSP_009752, VSP_009753;
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis and retina. In brain
CC highly expressed in the olfactory bulb, cortex and hippocampus and
CC lower level in thalamus, cerebellum and spinal cord. In brain it is
CC found in the perikaryon, dendrites, dendritic shafts, dendritic spines
CC and, excitatory and inhibitory synapses of neurons. In retina, it is
CC most abundant in the plexiform layers than in perikarya.
CC {ECO:0000269|PubMed:10436050, ECO:0000269|PubMed:12115684,
CC ECO:0000269|PubMed:9069286}.
CC -!- DEVELOPMENTAL STAGE: Detected in early embryonic stage as early as E15,
CC gradually increased throughout early development, peaked at
CC approximately between postnatal days P6 and P8, then slightly decreased
CC and remained relatively stable in the adult.
CC {ECO:0000269|PubMed:10436050}.
CC -!- DOMAIN: PDZ 6 mediates interaction with the PDZ recognition motif of
CC EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and
CC PDZ 5 mediate interaction with PRLHR (By similarity). PDZ 4 and PDZ 5
CC mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ 4, PDZ
CC 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction with PDZ
CC domain of GRASP1. PDZ 7 domain binds CSPG4. PDZ 6 mediates interaction
CC with the C-terminus of liprins-alpha. PDZ 1, PDZ 2 and PDZ 3 mediate
CC interaction with the PDZ-binding motif of FRAS1. {ECO:0000250,
CC ECO:0000269|PubMed:12458226}.
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DR EMBL; U88572; AAB51689.1; -; mRNA.
DR EMBL; AY437398; AAR08916.1; -; mRNA.
DR PIR; T32733; T32733.
DR RefSeq; NP_114458.1; NM_032069.1. [P97879-1]
DR PDB; 1M5Z; NMR; -; A=980-1070.
DR PDB; 1N7E; X-ray; 1.50 A; A=665-761.
DR PDB; 1N7F; X-ray; 1.80 A; A/B=665-761.
DR PDB; 1P1D; NMR; -; A=463-658.
DR PDB; 1P1E; NMR; -; A=463-563.
DR PDB; 2QT5; X-ray; 2.30 A; A/B=48-243.
DR PDBsum; 1M5Z; -.
DR PDBsum; 1N7E; -.
DR PDBsum; 1N7F; -.
DR PDBsum; 1P1D; -.
DR PDBsum; 1P1E; -.
DR PDBsum; 2QT5; -.
DR AlphaFoldDB; P97879; -.
DR SMR; P97879; -.
DR BioGRID; 249882; 11.
DR CORUM; P97879; -.
DR DIP; DIP-37486N; -.
DR ELM; P97879; -.
DR IntAct; P97879; 34.
DR MINT; P97879; -.
DR STRING; 10116.ENSRNOP00000005539; -.
DR BindingDB; P97879; -.
DR ChEMBL; CHEMBL2366484; -.
DR iPTMnet; P97879; -.
DR PhosphoSitePlus; P97879; -.
DR SwissPalm; P97879; -.
DR PaxDb; P97879; -.
DR PRIDE; P97879; -.
DR GeneID; 84016; -.
DR KEGG; rno:84016; -.
DR CTD; 23426; -.
DR RGD; 621667; Grip1.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; P97879; -.
DR OrthoDB; 65191at2759; -.
DR PhylomeDB; P97879; -.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR EvolutionaryTrace; P97879; -.
DR PRO; PR:P97879; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:InterPro.
DR GO; GO:0140059; P:dendrite arborization; IMP:RGD.
DR GO; GO:0007399; P:nervous system development; IMP:RGD.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:RGD.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IGI:ARUK-UCL.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:RGD.
DR Gene3D; 2.30.42.10; -; 7.
DR InterPro; IPR030026; GRIP1.
DR InterPro; IPR043545; GRIP1/2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR46227; PTHR46227; 1.
DR PANTHER; PTHR46227:SF3; PTHR46227:SF3; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 7.
DR SUPFAM; SSF50156; SSF50156; 7.
DR PROSITE; PS50106; PDZ; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse.
FT CHAIN 1..1112
FT /note="Glutamate receptor-interacting protein 1"
FT /id="PRO_0000083851"
FT DOMAIN 53..136
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 150..238
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 252..336
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 471..560
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 572..657
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 672..754
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 988..1070
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 752..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..416
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15226318"
FT /id="VSP_009751"
FT VAR_SEQ 417..451
FT /note="SSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSL -> MTPKRTEKEMKKP
FT HNFHHASHPPLRKGQKINAAHV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15226318"
FT /id="VSP_009752"
FT VAR_SEQ 1101..1112
FT /note="GNLETREPTNTL -> IPGDAVYFWQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15226318"
FT /id="VSP_009753"
FT CONFLICT 816
FT /note="R -> S (in Ref. 2; AAR08916)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="K -> Q (in Ref. 2; AAR08916)"
FT /evidence="ECO:0000305"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2QT5"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2QT5"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 144..156
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2QT5"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2QT5"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2QT5"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 228..239
FT /evidence="ECO:0007829|PDB:2QT5"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:1P1D"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:1P1D"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:1P1D"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 548..558
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:1P1D"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:1P1D"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:1P1D"
FT HELIX 635..644
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:1P1D"
FT STRAND 670..676
FT /evidence="ECO:0007829|PDB:1N7E"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:1N7E"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:1N7E"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:1N7E"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:1N7E"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:1N7E"
FT STRAND 744..751
FT /evidence="ECO:0007829|PDB:1N7E"
FT STRAND 985..992
FT /evidence="ECO:0007829|PDB:1M5Z"
FT STRAND 998..1006
FT /evidence="ECO:0007829|PDB:1M5Z"
FT STRAND 1013..1018
FT /evidence="ECO:0007829|PDB:1M5Z"
FT HELIX 1023..1027
FT /evidence="ECO:0007829|PDB:1M5Z"
FT STRAND 1034..1038
FT /evidence="ECO:0007829|PDB:1M5Z"
FT HELIX 1048..1056
FT /evidence="ECO:0007829|PDB:1M5Z"
FT STRAND 1061..1068
FT /evidence="ECO:0007829|PDB:1M5Z"
SQ SEQUENCE 1112 AA; 120298 MW; 2EFFFFE0D8609C59 CRC64;
MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG STVVELMKKE
GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY IKAVNGINLA KFRHDEIISL
LKNVGERVVL EVEYELPPVS IQGSSVMFRT VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV
VITCVRPGGP ADREGTIKPG DRLLSVDGIR LLGTTHAEAM SILKQCGQEA TLLIEYDVSV
MDSVATASGP LLVEVAKTPG ASLGVALTTS VCCNKQVIVI DKIKSASIAD RCGALHVGDH
ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI QRSDRQLPWD
PWASSQCSVH TNHHHNPHHP DHCRVPALGF PKALTPNSPP AMVSSSSPTS MSAYSLSSLN
MGTLPRSLYS TSPRGTMMRR RLKKKDFKSS LSLASSTVGL AGQVVHTETT EVVLTADPVT
GFGIQLQGSV FATETLSSPP LISYIEADSP AERCGVLQIG DRVMAINGIP TEDSTFEEAN
QLLRDSSITS KVTLEIEFDV AESVIPSSGT FHVKLPKKHS VELGITISSP SSRKPGDPLV
ISDIKKGSVA HRTGTLELGD KLLAIDNIRL DSCSMEDAVQ ILQQCEDLVK LKIRKDEDNS
DEQESSGAII YTVELKRYGG PLGITISGTE EPFDPIIISS LTKGGLAERT GAIHIGDRIL
AINSSSLKGK PLSEAIHLLQ MAGETVTLKI KKQTDAQPAS SPKKLPIPSH SSDLGDGEED
PSPIQRPGKL SDVYPSTVPS VDSAVDSWDG SGIDARYGSQ GTTFQTSGYN FNTYDWRSPK
KRASLSPVPK PRSQTYPDVG LSNEDWDRST ASGFAGASDS ADAEQEENFW SQALEDLETC
GQSGILRELE ATIMSGSTMS LNHEAPTARS QLGRQASFQE RSNSRPHYSQ TTRSNTLPSD
VGRKSVTLRK MKQEIKEIMS PTPVELHKVT LYKDSGMEDF GFSVADGLLE KGVYVKNIRP
AGPGDLGGLK PYDRLLQVNH VRTRDFDCCL VVPLIAESGN KLDLVISRNP LASQKSIEQP
ALPSDWSEQN SAFFQQPSHG GNLETREPTN TL
