MARK3_MOUSE
ID MARK3_MOUSE Reviewed; 753 AA.
AC Q03141; Q3TM40; Q3V1U3; Q8C6G9; Q8R375; Q9JKE4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=MAP/microtubule affinity-regulating kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=ELKL motif kinase 2;
DE Short=EMK-2;
DE AltName: Full=MPK-10;
GN Name=Mark3; Synonyms=Emk2, Mpk10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Darmon Y., Tornier C., Bessone S., Le Morvan V.;
RT "Mouse EMK2 (ELKL motif kinase 2).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Lung, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-753 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 180-234.
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=1281307;
RA Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A.,
RA Wilkinson D.G., Charnay P.;
RT "An Eph-related receptor protein tyrosine kinase gene segmentally expressed
RT in the developing mouse hindbrain.";
RL Oncogene 7:2499-2506(1992).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-374; SER-380;
RP SER-383; SER-400; SER-419; SER-540; SER-543 AND THR-549, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 659-753.
RX PubMed=17075132; DOI=10.1110/ps.062391106;
RA Tochio N., Koshiba S., Kobayashi N., Inoue M., Yabuki T., Aoki M., Seki E.,
RA Matsuda T., Tomo Y., Motoda Y., Kobayashi A., Tanaka A., Hayashizaki Y.,
RA Terada T., Shirouzu M., Kigawa T., Yokoyama S.;
RT "Solution structure of the kinase-associated domain 1 of mouse microtubule-
RT associated protein/microtubule affinity-regulating kinase 3.";
RL Protein Sci. 15:2534-2543(2006).
CC -!- FUNCTION: Serine/threonine-protein kinase. Involved in the specific
CC phosphorylation of microtubule-associated proteins for MAPT/TAU, MAP2
CC and MAP4. Phosphorylates CDC25C. Regulates localization and activity of
CC some histone deacetylases by mediating phosphorylation of HDAC7,
CC promoting subsequent interaction between HDAC7 and 14-3-3 and export
CC from the nucleus. Negatively regulates the Hippo signaling pathway and
CC antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to
CC inhibit the kinase activity of STK3/MST2 toward LATS1.
CC {ECO:0000250|UniProtKB:P27448}.
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 -!- 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 -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-211. Inhibited
CC by phosphorylation on Thr-564 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPT/TAU. Interacts with DLG5 (via coiled-coil
CC domain). Interacts with STK3/MST2 and STK4/MST1 in the presence of
CC DLG5. Interacts with YWHAB, YWHAG, YWHAQ and YWHAZ (By similarity).
CC {ECO:0000250|UniProtKB:P27448}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27448};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P27448}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:P27448}. Cytoplasm
CC {ECO:0000250|UniProtKB:P27448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q03141-1; Sequence=Displayed;
CC Name=2; Synonyms=ELKL motif kinase 2 short form;
CC IsoId=Q03141-2; Sequence=VSP_016140;
CC Name=3; Synonyms=ELKL motif kinase 2 long form;
CC IsoId=Q03141-3; Sequence=VSP_016141;
CC -!- PTM: Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation
CC at Thr-564 by PRKCZ/aPKC inhibits the kinase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26445.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF240783; AAF64456.1; -; mRNA.
DR EMBL; AK075742; BAC35922.1; ALT_INIT; mRNA.
DR EMBL; AK132247; BAE21056.1; -; mRNA.
DR EMBL; AK166157; BAE38602.1; -; mRNA.
DR EMBL; BC026445; AAH26445.1; ALT_INIT; mRNA.
DR EMBL; X57244; CAA40520.1; -; mRNA.
DR CCDS; CCDS26181.1; -. [Q03141-3]
DR CCDS; CCDS26182.1; -. [Q03141-2]
DR CCDS; CCDS88407.1; -. [Q03141-1]
DR PIR; S30496; S30496.
DR RefSeq; NP_067491.2; NM_021516.4. [Q03141-3]
DR RefSeq; NP_073712.2; NM_022801.4. [Q03141-2]
DR RefSeq; XP_006515578.1; XM_006515515.3.
DR PDB; 1UL7; NMR; -; A=659-753.
DR PDB; 1V5S; NMR; -; A=674-753.
DR PDBsum; 1UL7; -.
DR PDBsum; 1V5S; -.
DR AlphaFoldDB; Q03141; -.
DR BMRB; Q03141; -.
DR SMR; Q03141; -.
DR BioGRID; 201312; 15.
DR IntAct; Q03141; 4.
DR MINT; Q03141; -.
DR STRING; 10090.ENSMUSP00000082017; -.
DR iPTMnet; Q03141; -.
DR PhosphoSitePlus; Q03141; -.
DR EPD; Q03141; -.
DR jPOST; Q03141; -.
DR MaxQB; Q03141; -.
DR PaxDb; Q03141; -.
DR PeptideAtlas; Q03141; -.
DR PRIDE; Q03141; -.
DR ProteomicsDB; 292171; -. [Q03141-1]
DR ProteomicsDB; 292172; -. [Q03141-2]
DR ProteomicsDB; 292173; -. [Q03141-3]
DR Antibodypedia; 6515; 496 antibodies from 37 providers.
DR DNASU; 17169; -.
DR Ensembl; ENSMUST00000075281; ENSMUSP00000074757; ENSMUSG00000007411. [Q03141-2]
DR Ensembl; ENSMUST00000084953; ENSMUSP00000082017; ENSMUSG00000007411. [Q03141-3]
DR Ensembl; ENSMUST00000221459; ENSMUSP00000152483; ENSMUSG00000007411. [Q03141-1]
DR GeneID; 17169; -.
DR KEGG; mmu:17169; -.
DR UCSC; uc007pdk.2; mouse. [Q03141-3]
DR UCSC; uc007pdl.2; mouse. [Q03141-2]
DR UCSC; uc007pdm.2; mouse. [Q03141-1]
DR CTD; 4140; -.
DR MGI; MGI:1341865; Mark3.
DR VEuPathDB; HostDB:ENSMUSG00000007411; -.
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000154862; -.
DR HOGENOM; CLU_000288_157_5_1; -.
DR InParanoid; Q03141; -.
DR OMA; AKFRQGC; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q03141; -.
DR TreeFam; TF315213; -.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 17169; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Mark3; mouse.
DR EvolutionaryTrace; Q03141; -.
DR PRO; PR:Q03141; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q03141; protein.
DR Bgee; ENSMUSG00000007411; Expressed in undifferentiated genital tubercle and 262 other tissues.
DR ExpressionAtlas; Q03141; baseline and differential.
DR Genevisible; Q03141; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISS:UniProtKB.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; ISS:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:ARUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; ISS:ARUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033628; MARK3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346:SF1; PTHR24346:SF1; 2.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Cell projection; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..753
FT /note="MAP/microtubule affinity-regulating kinase 3"
FT /id="PRO_0000086305"
FT DOMAIN 56..307
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 326..365
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 695..744
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 62..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 211
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 564
FT /note="Phosphothreonine; by PKC/PRKCZ"
FT /evidence="ECO:0000250"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27448"
FT VAR_SEQ 615..638
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_016140"
FT VAR_SEQ 615..623
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_016141"
FT CONFLICT 333
FT /note="D -> V (in Ref. 2; BAC35922)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="N -> S (in Ref. 1; AAF64456)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="S -> G (in Ref. 2; BAC35922)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="D -> G (in Ref. 2; BAC35922)"
FT /evidence="ECO:0000305"
FT HELIX 672..685
FT /evidence="ECO:0007829|PDB:1UL7"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:1UL7"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:1UL7"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:1V5S"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:1UL7"
FT STRAND 711..719
FT /evidence="ECO:0007829|PDB:1UL7"
FT STRAND 721..735
FT /evidence="ECO:0007829|PDB:1UL7"
FT HELIX 737..750
FT /evidence="ECO:0007829|PDB:1UL7"
SQ SEQUENCE 753 AA; 84390 MW; B597BDD0398617CF CRC64;
MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK
TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE
VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK
AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG
VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ
IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT
YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD
HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK
ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS
THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG
STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSSEQKDEN REAKPRSLRF
TWSMKTTSSM DPSDMMREIR KVLDANNCDY EQRERFLLFC VHGDGHAENL VQWEMEVCKL
PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL
