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   27-MAR-2024, entry version 176.
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 15
CC       dpc, 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; 10116-ENSRNOP00000005539; -.
DR   GeneID; 84016; -.
DR   KEGG; rno:84016; -.
DR   AGR; RGD:621667; -.
DR   CTD; 23426; -.
DR   RGD; 621667; Grip1.
DR   eggNOG; KOG3528; Eukaryota.
DR   InParanoid; P97879; -.
DR   OrthoDB; 4199121at2759; -.
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:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR   GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000145; C:exocyst; IDA:RGD.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005874; C:microtubule; IDA: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:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098794; C:postsynapse; IDA:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR   GO; GO:0098793; C:presynapse; IDA:RGD.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR   GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR   GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR   GO; GO:0106033; C:spine synapse; IDA:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0043083; C:synaptic cleft; IDA:RGD.
DR   GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR   GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR   GO; GO:0051020; F:GTPase binding; IPI:RGD.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IDA:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR   GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IDA:RGD.
DR   GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
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:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR   GO; GO:0150012; P:positive regulation of neuron projection arborization; IMP:RGD.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:RGD.
DR   GO; GO:0008104; P:protein localization; ISO:RGD.
DR   GO; GO:0150092; P:regulation of synaptic scaling; IMP:RGD.
DR   GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:RGD.
DR   CDD; cd00992; PDZ_signaling; 7.
DR   Gene3D; 2.30.42.10; -; 7.
DR   InterPro; IPR043545; GRIP1/2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR46227:SF3; GLUTAMATE RECEPTOR-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR46227; GLUTAMATE RECEPTOR-INTERACTING PROTEIN GRIP; 1.
DR   Pfam; PF00595; PDZ; 6.
DR   Pfam; PF17820; PDZ_6; 1.
DR   SMART; SM00228; PDZ; 7.
DR   SUPFAM; SSF50156; PDZ domain-like; 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
//