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Database: UniProt
Entry: Q03555
LinkDB: Q03555
Original site: Q03555 
ID   GEPH_RAT                Reviewed;         768 AA.
AC   Q03555;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 3.
DT   06-JUL-2016, entry version 167.
DE   RecName: Full=Gephyrin;
DE   AltName: Full=Putative glycine receptor-tubulin linker protein;
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase;
DE              Short=MPT adenylyltransferase;
DE              EC=2.7.7.75 {ECO:0000305|PubMed:9990024};
DE     AltName: Full=Domain G;
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase;
DE              Short=MPT Mo-transferase;
DE              EC=2.10.1.1 {ECO:0000305|PubMed:9990024};
DE     AltName: Full=Domain E;
GN   Name=Gphn; Synonyms=Gph;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=1319186; DOI=10.1016/0896-6273(92)90136-2;
RA   Prior P., Schmitt B., Grenningloh G., Pribilla I., Multhaup G.,
RA   Beyreuther K., Maulet Y., Werner P., Langosch D., Kirsch J., Betz H.;
RT   "Primary structure and alternative splice variants of gephyrin, a
RT   putative glycine receptor-tubulin linker protein.";
RL   Neuron 8:1161-1170(1992).
RN   [2]
RP   SEQUENCE REVISION TO 255.
RA   Schmitt B.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP   INTERACTION WITH GLRB.
RX   PubMed=11083919; DOI=10.1006/mcne.2000.0899;
RA   Meier J., De Chaldee M., Triller A., Vannier C.;
RT   "Functional heterogeneity of gephyrins.";
RL   Mol. Cell. Neurosci. 16:566-577(2000).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, X-RAY
RP   CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 348-768 IN COMPLEX WITH GLRB, AND
RP   SUBUNIT.
RX   PubMed=15201864; DOI=10.1038/sj.emboj.7600256;
RA   Sola M., Bavro V.N., Timmins J., Franz T., Ricard-Blum S., Schoehn G.,
RA   Ruigrok R.W.H., Paarmann I., Saiyed T., O'Sullivan G.A., Schmitt B.,
RA   Betz H., Weissenhorn W.;
RT   "Structural basis of dynamic glycine receptor clustering by
RT   gephyrin.";
RL   EMBO J. 23:2510-2519(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=8264797; DOI=10.1038/366745a0;
RA   Kirsch J., Wolters I., Triller A., Betz H.;
RT   "Gephyrin antisense oligonucleotides prevent glycine receptor
RT   clustering in spinal neurons.";
RL   Nature 366:745-748(1993).
RN   [6]
RP   INTERACTION WITH GABARAP.
RX   PubMed=10900017; DOI=10.1073/pnas.97.15.8594;
RA   Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H.,
RA   Olsen R.W., Betz H.;
RT   "The gamma-aminobutyric acid type A receptor (GABAAR)-associated
RT   protein GABARAP interacts with gephyrin but is not involved in
RT   receptor anchoring at the synapse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000).
RN   [7]
RP   FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX   PubMed=9990024; DOI=10.1073/pnas.96.4.1333;
RA   Stallmeyer B., Schwarz G., Schulze J., Nerlich A., Reiss J.,
RA   Kirsch J., Mendel R.R.;
RT   "The neurotransmitter receptor-anchoring protein gephyrin
RT   reconstitutes molybdenum cofactor biosynthesis in bacteria, plants,
RT   and mammalian cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1333-1338(1999).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12684523; DOI=10.1074/jbc.M301070200;
RA   Rees M.I., Harvey K., Ward H., White J.H., Evans L., Duguid I.C.,
RA   Hsu C.-C., Coleman S.L., Miller J., Baer K., Waldvogel H.J.,
RA   Gibbon F., Smart T.G., Owen M.J., Harvey R.J., Snell R.G.;
RT   "Isoform heterogeneity of the human gephyrin gene (GPHN), binding
RT   domains to the glycine receptor, and mutation analysis in
RT   hyperekplexia.";
RL   J. Biol. Chem. 278:24688-24696(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-207 AND
RP   SER-283, 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.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, AND SUBUNIT.
RX   PubMed=11325967; DOI=10.1074/jbc.M101923200;
RA   Sola M., Kneussel M., Heck I.S., Betz H., Weissenhorn W.;
RT   "X-ray crystal structure of the trimeric N-terminal domain of
RT   gephyrin.";
RL   J. Biol. Chem. 276:25294-25301(2001).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 350-768 IN COMPLEX WITH GLRB,
RP   SUBCELLULAR LOCATION, INTERACTION WITH GLRB, AND MUTAGENESIS OF
RP   PHE-362; PRO-745 AND 745-PRO-PRO-746.
RX   PubMed=16511563; DOI=10.1038/sj.emboj.7601029;
RA   Kim E.Y., Schrader N., Smolinsky B., Bedet C., Vannier C., Schwarz G.,
RA   Schindelin H.;
RT   "Deciphering the structural framework of glycine receptor anchoring by
RT   gephyrin.";
RL   EMBO J. 25:1385-1395(2006).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-768, INTERACTION WITH
RP   GLRB, AND SUBUNIT.
RX   PubMed=25137389; DOI=10.1021/cb500303a;
RA   Maric H.M., Kasaragod V.B., Schindelin H.;
RT   "Modulation of gephyrin-glycine receptor affinity by multivalency.";
RL   ACS Chem. Biol. 9:2554-2562(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 350-768 IN COMPLEX WITH
RP   GABRA3, INTERACTION WITH GABRA3 AND GLRB, AND SUBUNIT.
RX   PubMed=25531214; DOI=10.1038/ncomms6767;
RA   Maric H.M., Kasaragod V.B., Hausrat T.J., Kneussel M., Tretter V.,
RA   Stromgaard K., Schindelin H.;
RT   "Molecular basis of the alternative recruitment of GABA(A) versus
RT   glycine receptors through gephyrin.";
RL   Nat. Commun. 5:5767-5767(2014).
CC   -!- FUNCTION: Microtubule-associated protein involved in membrane
CC       protein-cytoskeleton interactions. It is thought to anchor the
CC       inhibitory glycine receptor (GLYR) to subsynaptic microtubules
CC       (PubMed:8264797). Catalyzes two steps in the biosynthesis of the
CC       molybdenum cofactor. In the first step, molybdopterin is
CC       adenylated. Subsequently, molybdate is inserted into adenylated
CC       molybdopterin and AMP is released (PubMed:9990024).
CC       {ECO:0000269|PubMed:8264797, ECO:0000269|PubMed:9990024}.
CC   -!- CATALYTIC ACTIVITY: ATP + molybdopterin = diphosphate + adenylyl-
CC       molybdopterin. {ECO:0000305|PubMed:9990024}.
CC   -!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate =
CC       molybdenum cofactor + AMP. {ECO:0000305|PubMed:9990024}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ENZYME REGULATION: Inhibited by copper and tungsten.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000305|PubMed:9990024}.
CC   -!- SUBUNIT: Homotrimer, homodimer and homooligomer (PubMed:11325967,
CC       PubMed:25137389, PubMed:25531214). Interacts with SRGAP2 (via SH3
CC       domain) (By similarity). Interacts with GLRB (PubMed:15201864,
CC       PubMed:16511563, PubMed:25137389, PubMed:25531214). Interacts with
CC       GABARAP (PubMed:10900017). Interacts with GABRA3
CC       (PubMed:25531214). GABRA3 and GLRB occupy overlapping binding
CC       sites (PubMed:25531214). {ECO:0000250|UniProtKB:Q8BUV3,
CC       ECO:0000269|PubMed:10900017, ECO:0000269|PubMed:11325967,
CC       ECO:0000269|PubMed:15201864, ECO:0000269|PubMed:16511563}.
CC   -!- INTERACTION:
CC       P20236:Gabra3; NbExp=5; IntAct=EBI-5273276, EBI-5273284;
CC       P48168:Glrb (xeno); NbExp=4; IntAct=EBI-349317, EBI-7069198;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse
CC       {ECO:0000269|PubMed:16511563}. Cell junction, synapse,
CC       postsynaptic cell membrane {ECO:0000269|PubMed:16511563};
CC       Peripheral membrane protein {ECO:0000269|PubMed:16511563};
CC       Cytoplasmic side {ECO:0000269|PubMed:16511563}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:16511563}. Cell membrane
CC       {ECO:0000269|PubMed:12684523}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12684523}; Cytoplasmic side
CC       {ECO:0000269|PubMed:12684523}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q9NQX3}. Note=Cytoplasmic face of
CC       glycinergic postsynaptic membranes. {ECO:0000269|PubMed:16511563}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=6;
CC         IsoId=Q03555-1; Sequence=Displayed;
CC       Name=1; Synonyms=GE124'56;
CC         IsoId=Q03555-2; Sequence=VSP_003238;
CC       Name=2; Synonyms=GE236;
CC         IsoId=Q03555-3; Sequence=VSP_003239, VSP_003240, VSP_003243;
CC       Name=3; Synonyms=GE24'6;
CC         IsoId=Q03555-4; Sequence=VSP_003239;
CC       Name=4; Synonyms=GE245;
CC         IsoId=Q03555-5; Sequence=VSP_003241, VSP_003242;
CC       Name=5; Synonyms=GE26;
CC         IsoId=Q03555-6; Sequence=VSP_003239, VSP_003243;
CC   -!- TISSUE SPECIFICITY: Expressed in tissues including spinal cord,
CC       brain, liver, kidney and lung.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC       {ECO:0000305}.
DR   EMBL; X66366; CAA47009.2; -; mRNA.
DR   PIR; JH0681; JH0681.
DR   RefSeq; NP_074056.2; NM_022865.3. [Q03555-6]
DR   UniGene; Rn.11032; -.
DR   PDB; 1IHC; X-ray; 1.90 A; A=1-201.
DR   PDB; 1T3E; X-ray; 3.25 A; A/B=348-768.
DR   PDB; 2FTS; X-ray; 2.41 A; A=350-768.
DR   PDB; 2FU3; X-ray; 2.70 A; A/B=350-768.
DR   PDB; 4PD0; X-ray; 1.70 A; A=350-768.
DR   PDB; 4PD1; X-ray; 1.98 A; A=350-768.
DR   PDB; 4TK1; X-ray; 2.70 A; A/B=350-768.
DR   PDB; 4TK2; X-ray; 4.10 A; A/B=350-768.
DR   PDB; 4TK3; X-ray; 2.70 A; A/B=350-768.
DR   PDB; 4TK4; X-ray; 3.60 A; A/B=350-768.
DR   PDB; 4U90; X-ray; 2.00 A; A=350-768.
DR   PDB; 4U91; X-ray; 2.00 A; A=350-768.
DR   PDB; 5ERQ; X-ray; 1.55 A; A=350-768.
DR   PDB; 5ERR; X-ray; 1.65 A; A=350-768.
DR   PDB; 5ERS; X-ray; 1.70 A; A=350-768.
DR   PDB; 5ERT; X-ray; 2.00 A; A=350-768.
DR   PDB; 5ERU; X-ray; 1.60 A; A=350-768.
DR   PDB; 5ERV; X-ray; 1.80 A; A=350-768.
DR   PDBsum; 1IHC; -.
DR   PDBsum; 1T3E; -.
DR   PDBsum; 2FTS; -.
DR   PDBsum; 2FU3; -.
DR   PDBsum; 4PD0; -.
DR   PDBsum; 4PD1; -.
DR   PDBsum; 4TK1; -.
DR   PDBsum; 4TK2; -.
DR   PDBsum; 4TK3; -.
DR   PDBsum; 4TK4; -.
DR   PDBsum; 4U90; -.
DR   PDBsum; 4U91; -.
DR   PDBsum; 5ERQ; -.
DR   PDBsum; 5ERR; -.
DR   PDBsum; 5ERS; -.
DR   PDBsum; 5ERT; -.
DR   PDBsum; 5ERU; -.
DR   PDBsum; 5ERV; -.
DR   ProteinModelPortal; Q03555; -.
DR   SMR; Q03555; 13-194, 350-768.
DR   BioGrid; 249211; 8.
DR   DIP; DIP-33263N; -.
DR   IntAct; Q03555; 5.
DR   MINT; MINT-241818; -.
DR   iPTMnet; Q03555; -.
DR   PhosphoSite; Q03555; -.
DR   SwissPalm; Q03555; -.
DR   PRIDE; Q03555; -.
DR   GeneID; 64845; -.
DR   KEGG; rno:64845; -.
DR   UCSC; RGD:69194; rat. [Q03555-1]
DR   CTD; 10243; -.
DR   RGD; 69194; Gphn.
DR   HOGENOM; HOG000280651; -.
DR   HOVERGEN; HBG005828; -.
DR   InParanoid; Q03555; -.
DR   KO; K15376; -.
DR   PhylomeDB; Q03555; -.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; Q03555; -.
DR   PRO; PR:Q03555; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IDA:MGI.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IDA:MGI.
DR   GO; GO:0030674; F:protein binding, bridging; TAS:RGD.
DR   GO; GO:0032947; F:protein complex scaffold; IDA:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
DR   GO; GO:0005102; F:receptor binding; IPI:RGD.
DR   GO; GO:0015631; F:tubulin binding; TAS:RGD.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR   GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:UniProtKB.
DR   GO; GO:0072579; P:glycine receptor clustering; IBA:GO_Central.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:MGI.
DR   GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
DR   GO; GO:0006605; P:protein targeting; TAS:RGD.
DR   GO; GO:0007416; P:synapse assembly; IEP:RGD.
DR   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 2.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 2.
DR   SUPFAM; SSF53218; SSF53218; 2.
DR   SUPFAM; SSF63867; SSF63867; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell junction;
KW   Cell membrane; Cell projection; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Magnesium; Membrane;
KW   Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Transferase.
FT   CHAIN         1    768       Gephyrin.
FT                                /FTId=PRO_0000170965.
FT   REGION       14    166       MPT Mo-transferase.
FT   REGION      153    348       Interaction with GABARAP.
FT   REGION      326    768       MPT adenylyltransferase.
FT   COMPBIAS    213    218       Glu-rich (acidic).
FT   MOD_RES     201    201       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     207    207       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     211    211       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NQX3}.
FT   MOD_RES     213    213       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8BUV3}.
FT   MOD_RES     275    275       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8BUV3}.
FT   MOD_RES     278    278       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8BUV3}.
FT   MOD_RES     279    279       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NQX3}.
FT   MOD_RES     281    281       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8BUV3}.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     337    337       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NQX3}.
FT   VAR_SEQ       1     22       MATEGMILTNHDHQIRVGVLTV -> MSFPLSPAFTLLHIL
FT                                V (in isoform 1).
FT                                {ECO:0000303|PubMed:11083919}.
FT                                /FTId=VSP_003238.
FT   VAR_SEQ      99    111       Missing (in isoform 5, isoform 2 and
FT                                isoform 3). {ECO:0000303|PubMed:11083919,
FT                                ECO:0000303|PubMed:1319186}.
FT                                /FTId=VSP_003239.
FT   VAR_SEQ     256    256       K -> KNHPFYTSPAVFMANHGQPIPGLISYSHHATGSADK
FT                                R (in isoform 2).
FT                                {ECO:0000303|PubMed:11083919}.
FT                                /FTId=VSP_003240.
FT   VAR_SEQ     302    320       Missing (in isoform 5 and isoform 2).
FT                                {ECO:0000303|PubMed:11083919,
FT                                ECO:0000303|PubMed:1319186}.
FT                                /FTId=VSP_003243.
FT   VAR_SEQ     302    315       QIRRPDESKGVASR -> ARLPSCSSTYSVSE (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:11083919}.
FT                                /FTId=VSP_003241.
FT   VAR_SEQ     316    320       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11083919}.
FT                                /FTId=VSP_003242.
FT   MUTAGEN     362    362       F->A: Reduced GLRB binding.
FT                                {ECO:0000269|PubMed:16511563}.
FT   MUTAGEN     745    746       PP->AA: Reduced GLRB binding.
FT                                {ECO:0000269|PubMed:16511563}.
FT   MUTAGEN     745    745       P->A: Loss of GLRB binding.
FT                                {ECO:0000269|PubMed:16511563}.
FT   CONFLICT    255    255       A -> R (in Ref. 3). {ECO:0000305}.
FT   STRAND       16     22       {ECO:0000244|PDB:1IHC}.
FT   HELIX        24     27       {ECO:0000244|PDB:1IHC}.
FT   HELIX        34     44       {ECO:0000244|PDB:1IHC}.
FT   TURN         46     49       {ECO:0000244|PDB:1IHC}.
FT   STRAND       52     59       {ECO:0000244|PDB:1IHC}.
FT   HELIX        63     75       {ECO:0000244|PDB:1IHC}.
FT   STRAND       80     86       {ECO:0000244|PDB:1IHC}.
FT   STRAND       89     91       {ECO:0000244|PDB:1IHC}.
FT   HELIX       112    116       {ECO:0000244|PDB:1IHC}.
FT   STRAND      118    120       {ECO:0000244|PDB:1IHC}.
FT   HELIX       122    135       {ECO:0000244|PDB:1IHC}.
FT   HELIX       137    141       {ECO:0000244|PDB:1IHC}.
FT   STRAND      146    149       {ECO:0000244|PDB:1IHC}.
FT   STRAND      152    157       {ECO:0000244|PDB:1IHC}.
FT   HELIX       161    171       {ECO:0000244|PDB:1IHC}.
FT   HELIX       172    174       {ECO:0000244|PDB:1IHC}.
FT   HELIX       175    182       {ECO:0000244|PDB:1IHC}.
FT   HELIX       188    193       {ECO:0000244|PDB:1IHC}.
FT   STRAND      355    357       {ECO:0000244|PDB:4U90}.
FT   HELIX       358    368       {ECO:0000244|PDB:4PD0}.
FT   STRAND      374    378       {ECO:0000244|PDB:4PD0}.
FT   HELIX       379    381       {ECO:0000244|PDB:4PD0}.
FT   STRAND      386    389       {ECO:0000244|PDB:4PD0}.
FT   STRAND      397    400       {ECO:0000244|PDB:4PD0}.
FT   STRAND      402    410       {ECO:0000244|PDB:4PD0}.
FT   HELIX       412    414       {ECO:0000244|PDB:4PD0}.
FT   STRAND      416    425       {ECO:0000244|PDB:4PD0}.
FT   STRAND      439    443       {ECO:0000244|PDB:4PD0}.
FT   STRAND      455    458       {ECO:0000244|PDB:4PD0}.
FT   HELIX       459    461       {ECO:0000244|PDB:4PD0}.
FT   STRAND      462    467       {ECO:0000244|PDB:4PD0}.
FT   TURN        469    471       {ECO:0000244|PDB:2FU3}.
FT   STRAND      473    479       {ECO:0000244|PDB:4PD0}.
FT   TURN        485    488       {ECO:0000244|PDB:4PD0}.
FT   STRAND      494    496       {ECO:0000244|PDB:4PD0}.
FT   STRAND      501    503       {ECO:0000244|PDB:4PD0}.
FT   HELIX       511    520       {ECO:0000244|PDB:4PD0}.
FT   STRAND      524    528       {ECO:0000244|PDB:4PD0}.
FT   STRAND      533    538       {ECO:0000244|PDB:4PD0}.
FT   HELIX       558    568       {ECO:0000244|PDB:4PD0}.
FT   STRAND      573    579       {ECO:0000244|PDB:4PD0}.
FT   HELIX       583    596       {ECO:0000244|PDB:4PD0}.
FT   STRAND      598    605       {ECO:0000244|PDB:4PD0}.
FT   STRAND      607    610       {ECO:0000244|PDB:4PD0}.
FT   HELIX       613    620       {ECO:0000244|PDB:4PD0}.
FT   STRAND      625    632       {ECO:0000244|PDB:4PD0}.
FT   STRAND      640    646       {ECO:0000244|PDB:4PD0}.
FT   STRAND      649    656       {ECO:0000244|PDB:4PD0}.
FT   HELIX       660    669       {ECO:0000244|PDB:4PD0}.
FT   HELIX       671    678       {ECO:0000244|PDB:4PD0}.
FT   STRAND      688    695       {ECO:0000244|PDB:4PD0}.
FT   STRAND      704    711       {ECO:0000244|PDB:4PD0}.
FT   STRAND      716    718       {ECO:0000244|PDB:1T3E}.
FT   STRAND      720    723       {ECO:0000244|PDB:4PD0}.
FT   STRAND      728    730       {ECO:0000244|PDB:2FTS}.
FT   HELIX       731    735       {ECO:0000244|PDB:4PD0}.
FT   STRAND      740    744       {ECO:0000244|PDB:4PD0}.
FT   STRAND      752    754       {ECO:0000244|PDB:4PD1}.
FT   STRAND      759    764       {ECO:0000244|PDB:4PD0}.
SQ   SEQUENCE   768 AA;  83266 MW;  FAD1B6DD76ED79EA CRC64;
     MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
     DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEKF PTFPFCGLQK GATKEVIERE
     APGMALAMLM GSLNVTPLGM LSRPVCGIRG KTLIINLPGS KKGSQECFQF ILPALPHAID
     LLRDAIVKVK EVHDELEDLP SPPPPLSPPP TTSPHKQTED KGVQCEEEEE EKKDSGVAST
     EDSSSSHITA AALAAKIPDS IISRGVQVLP RDTASLSTTP SESPRAQATS RLSTASCPTP
     KQIRRPDESK GVASRVGSLK VQSRCSSKEN ILRASHSAVD ITKVARRHRM SPFPLTSMDK
     AFITVLEMTP VLGTEIINYR DGMGRVLAQD VYAKDNLPPF PASVKDGYAV RAADGPGDRF
     IIGESQAGEQ PTQTVMPGQV MRVTTGAPIP CGADAVVQVE DTELIRESDD GTEELEVRIL
     VQARPGQDIR PIGHDIKRGE CVLAKGTHMG PSEIGLLATV GVTEVEVNKF PVVAVMSTGN
     ELLNPEDDLL PGKIRDSNRS TLLATIQEHG YPTINLGIVG DNPDDLLNAL NEGISRADVI
     ITSGGVSMGE KDYLKQVLDI DLHAQIHFGR VFMKPGLPTT FATLDIDGVR KIIFALPGNP
     VSAVVTCNLF VVPALRKMQG ILDPRPTIIK ARLSCDVKLD PRPEYHRCIL TWHHQEPLPW
     AQSTGNQMSS RLMSMRSANG LLMLPPKTEQ YVELHKGEVV DVMVIGRL
//
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