CSKP_RAT
ID CSKP_RAT Reviewed; 909 AA.
AC Q62915;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peripheral plasma membrane protein CASK {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:O14936};
DE AltName: Full=Calcium/calmodulin-dependent serine protein kinase;
GN Name=Cask {ECO:0000312|RGD:62004};
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], INTERACTION WITH NEUREXINS, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA Hata Y., Butz S., Suedhof T.C.;
RT "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT protein kinase domain identified by interaction with neurexins.";
RL J. Neurosci. 16:2488-2494(1996).
RN [2]
RP INTERACTION WITH APBA1 AND LIN7.
RC TISSUE=Testis;
RX PubMed=9753324; DOI=10.1016/s0092-8674(00)81736-5;
RA Butz S., Okamoto M., Suedhof T.C.;
RT "A tripartite protein complex with the potential to couple synaptic vesicle
RT exocytosis to cell adhesion in brain.";
RL Cell 94:773-782(1998).
RN [3]
RP FUNCTION, INTERACTION WITH TBR1, AND SUBCELLULAR LOCATION.
RX PubMed=10749215; DOI=10.1038/35005118;
RA Hsueh Y.P., Wang T.F., Yang F.C., Sheng M.;
RT "Nuclear translocation and transcription regulation by the membrane-
RT associated guanylate kinase CASK/LIN-2.";
RL Nature 404:298-302(2000).
RN [4]
RP INTERACTION WITH CASKIN1; LIN7A; LIN7B; LIN7C; APBA1 AND NRXN1.
RX PubMed=12040031; DOI=10.1523/jneurosci.22-11-04264.2002;
RA Tabuchi K., Biederer T., Butz S., Suedhof T.C.;
RT "CASK participates in alternative tripartite complexes in which Mint 1
RT competes for binding with Caskin 1, a novel CASK-binding protein.";
RL J. Neurosci. 22:4264-4273(2002).
RN [5]
RP INTERACTION WITH DLG1 AND DLG4.
RX PubMed=12151521; DOI=10.1523/jneurosci.22-15-06415.2002;
RA Chetkovich D.M., Bunn R.C., Kuo S.-H., Kawasaki Y., Kohwi M., Bredt D.S.;
RT "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by
RT distinct mechanisms.";
RL J. Neurosci. 22:6415-6425(2002).
RN [6]
RP INTERACTION WITH DLG1.
RX PubMed=11865057; DOI=10.1128/mcb.22.6.1778-1791.2002;
RA Lee S., Fan S., Makarova O., Straight S., Margolis B.;
RT "A novel and conserved protein-protein interaction domain of mammalian Lin-
RT 2/CASK binds and recruits SAP97 to the lateral surface of epithelia.";
RL Mol. Cell. Biol. 22:1778-1791(2002).
RN [7]
RP INTERACTION WITH WHRN, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12641734; DOI=10.1046/j.1471-4159.2003.01647.x;
RA Yap C.C., Liang F., Yamazaki Y., Muto Y., Kishida H., Hayashida T.,
RA Hashikawa T., Yano R.;
RT "CIP98, a novel PDZ domain protein, is expressed in the central nervous
RT system and interacts with calmodulin-dependent serine kinase.";
RL J. Neurochem. 85:123-134(2003).
RN [8]
RP INTERACTION WITH FCHSD2.
RX PubMed=14627983; DOI=10.1038/sj.onc.1206996;
RA Ohno H., Hirabayashi S., Kansaku A., Yao I., Tajima M., Nishimura W.,
RA Ohnishi H., Mashima H., Fujita T., Omata M., Hata Y.;
RT "Carom: a novel membrane-associated guanylate kinase-interacting protein
RT with two SH3 domains.";
RL Oncogene 22:8422-8431(2003).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH ACTN4; IQGAP1; MAGI2; NPHS1; SPTAN1 AND
RP SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Renal glomerulus;
RX PubMed=15994232; DOI=10.1073/pnas.0504166102;
RA Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G.;
RT "Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and
RT alpha-actinin are components of the nephrin multiprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005).
RN [10]
RP INTERACTION WITH NRXN1.
RX PubMed=25385611; DOI=10.1073/pnas.1416515111;
RA Li Y., Wei Z., Yan Y., Wan Q., Du Q., Zhang M.;
RT "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem
RT reveals a highly specific assembly mechanism for the apical Crumbs
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17444-17449(2014).
RN [11]
RP STRUCTURE BY NMR OF 339-394 IN COMPLEX WITH DLG1.
RX PubMed=15048107; DOI=10.1038/nsmb751;
RA Feng W., Long J.F., Fan J.S., Suetake T., Zhang M.;
RT "The tetrameric L27 domain complex as an organization platform for
RT supramolecular assemblies.";
RL Nat. Struct. Mol. Biol. 11:475-480(2004).
CC -!- FUNCTION: Multidomain scaffolding Mg(2+)-independent protein kinase
CC that catalyzes the phosphotransfer from ATP to proteins such as NRXN1,
CC and plays a role in synaptic transmembrane protein anchoring and ion
CC channel trafficking (By similarity). Multidomain scaffolding protein
CC with a role in synaptic transmembrane protein anchoring and ion channel
CC trafficking.ontributes to neural development and regulation of gene
CC expression via interaction with the transcription factor TBR1. Binds to
CC cell-surface proteins, including amyloid precursor protein, neurexins,
CC and syndecans. May mediate a link between the extracellular matrix and
CC the actin cytoskeleton via its interaction with syndecan and with the
CC actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7
CC complex, which associates with the motor protein KIF17 to transport
CC vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B
CC along microtubules (By similarity). {ECO:0000250|UniProtKB:O14936,
CC ECO:0000250|UniProtKB:O70589, ECO:0000269|PubMed:10749215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:O14936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:O14936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Note=Unlike other protein kinases, does not require a divalent cation
CC such as magnesium for catalytic activity. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Differs from archetypal CaMK members in that the
CC kinase domain exhibits a constitutively active conformation and the
CC autoinhibitory region does not engage in direct contact with the ATP-
CC binding cleft, although it still binds Ca(2+)/CAM. {ECO:0000250}.
CC -!- SUBUNIT: CASK and LIN7 form two mutually exclusive tripartite complexes
CC with APBA1 or CASKIN1 (PubMed:12040031). Component of the brain-
CC specific heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex) composed
CC of at least APBA1, CASK, and LIN7, which associates with the motor
CC protein KIF17 to transport vesicles along microtubules (By similarity).
CC Forms a heterotrimeric complex with DLG1 and LIN7B via their L27
CC domains (By similarity). Identified in a complex with ACTN4, IQGAP1,
CC MAGI2, NPHS1, SPTAN1 and SPTBN1 (PubMed:15994232). Part of a complex
CC containing CASK, TBR1 and TSPYL2 (By similarity). Interacts with WHRN
CC (PubMed:12641734). Interacts (via the PDZ, SH3 and guanylate kinase-
CC like domains) with NRXN1 (via C-terminus) (PubMed:8786425,
CC PubMed:25385611). Interacts with CASKIN1, APBA1, LIN7(A/B/C), and L27
CC domain of DLG1 and isoform 2 of DLG4 (PubMed:9753324, PubMed:12040031,
CC PubMed:12151521, PubMed:11865057, PubMed:15048107). Interacts with
CC FCHSD2 (PubMed:14627983). Interacts with KIRREL3 (By similarity).
CC Interacts with TBR1 (PubMed:10749215). Interacts with TSPYL2 (By
CC similarity). {ECO:0000250|UniProtKB:O14936,
CC ECO:0000250|UniProtKB:O70589, ECO:0000269|PubMed:10749215,
CC ECO:0000269|PubMed:11865057, ECO:0000269|PubMed:12040031,
CC ECO:0000269|PubMed:12151521, ECO:0000269|PubMed:12641734,
CC ECO:0000269|PubMed:14627983, ECO:0000269|PubMed:15048107,
CC ECO:0000269|PubMed:15994232, ECO:0000269|PubMed:25385611,
CC ECO:0000269|PubMed:8786425, ECO:0000269|PubMed:9753324}.
CC -!- INTERACTION:
CC Q62915; O94868: FCHSD2; Xeno; NbExp=2; IntAct=EBI-704635, EBI-1215612;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749215}. Cytoplasm
CC {ECO:0000269|PubMed:12641734, ECO:0000269|PubMed:15994232}. Cell
CC membrane {ECO:0000269|PubMed:14627983}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14627983}.
CC -!- TISSUE SPECIFICITY: Expressed in the foot process layer of podocytes in
CC the kidney glomerulus and in tubules (at protein level). Detected in
CC brain and neurons. {ECO:0000269|PubMed:12641734,
CC ECO:0000269|PubMed:15994232, ECO:0000269|PubMed:8786425}.
CC -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain
CC probably binds LIN7. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain mediates the interaction with FCHSD2.
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; U47110; AAB19127.1; -; mRNA.
DR RefSeq; NP_071520.1; NM_022184.1.
DR PDB; 1RSO; NMR; -; B/D=339-394.
DR PDB; 6LNM; X-ray; 2.40 A; A/C/E=1-345.
DR PDBsum; 1RSO; -.
DR PDBsum; 6LNM; -.
DR AlphaFoldDB; Q62915; -.
DR SMR; Q62915; -.
DR BioGRID; 248269; 12.
DR CORUM; Q62915; -.
DR ELM; Q62915; -.
DR IntAct; Q62915; 8.
DR MINT; Q62915; -.
DR iPTMnet; Q62915; -.
DR PhosphoSitePlus; Q62915; -.
DR SwissPalm; Q62915; -.
DR jPOST; Q62915; -.
DR PaxDb; Q62915; -.
DR PRIDE; Q62915; -.
DR ABCD; Q62915; 1 sequenced antibody.
DR GeneID; 29647; -.
DR KEGG; rno:29647; -.
DR UCSC; RGD:62004; rat.
DR CTD; 8573; -.
DR RGD; 62004; Cask.
DR eggNOG; KOG0609; Eukaryota.
DR InParanoid; Q62915; -.
DR OrthoDB; 95102at2759; -.
DR PhylomeDB; Q62915; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR EvolutionaryTrace; Q62915; -.
DR PRO; PR:Q62915; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0060170; C:ciliary membrane; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005652; C:nuclear lamina; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098846; C:podocyte foot; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0070509; P:calcium ion import; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0090288; P:negative regulation of cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:RGD.
DR CDD; cd12081; SH3_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calmodulin-binding; Cell membrane; Cytoplasm;
KW Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain;
KW Transferase.
FT CHAIN 1..909
FT /note="Peripheral plasma membrane protein CASK"
FT /id="PRO_0000094570"
FT DOMAIN 12..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..398
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 402..455
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 489..564
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 600..670
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 722..894
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 305..315
FT /note="Calmodulin-binding"
FT REGION 482..909
FT /note="Required for interaction with NRXN1 (via C-terminal
FT tail)"
FT /evidence="ECO:0000269|PubMed:25385611"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 151
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 155
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70589"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14936"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:6LNM"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:6LNM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:6LNM"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6LNM"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:6LNM"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1RSO"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:1RSO"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:1RSO"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:1RSO"
SQ SEQUENCE 909 AA; 103259 MW; 3694A9A44AC29629 CRC64;
MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK
REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH
YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV
GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR
QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA
RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL
TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP
ENNDAKELKR ILTQPHFMAL LQTHHVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM
DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN
GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS
VSIYVRAQFE YDPAKDDLIP CKEAGIRFRV GDIIQIISKD DHNWWQGKLE NSKNGTAGLI
PSPELQEWRV ACIAMEKTKQ EQQASCTWFG KKKKQYKDKY LAKHNADLVT YEEVVKLPAF
KRKTLVLLGA HGVGRRHIKN TLITKHPERF AYPIPHTTRP PKKDEENGKN YYFVSHDQMM
QDISNNEYLE YGSHEDAMYG TKLETIRKIH EQGLIAILDV EPQALKVLRT AEFPPFVVFI
AAPTITPGLN EDESLQRLQK ESDVLQRTYA HYFDLTIINN EIDETIRHLE EAVELVCTAP
QWVPVSWVY
