CSKI2_HUMAN
ID CSKI2_HUMAN Reviewed; 1202 AA.
AC Q8WXE0; B4DTT3; B7Z9H1; Q7LG69; Q9ULT1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Caskin-2;
DE AltName: Full=CASK-interacting protein 2;
GN Name=CASKIN2; Synonyms=KIAA1139;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-891.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-891.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-891.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-1202 (ISOFORM 1), AND VARIANT
RP GLY-891.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-396; SER-471;
RP SER-858 AND SER-892, VARIANT [LARGE SCALE ANALYSIS] GLY-891, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396 AND SER-471, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253; SER-358; SER-393;
RP SER-396; SER-471; SER-725; SER-858; SER-878 AND SER-892, VARIANT [LARGE
RP SCALE ANALYSIS] GLY-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP STRUCTURE BY NMR OF 284-348.
RX PubMed=21328705; DOI=10.1142/s0219720011005276;
RA Alipanahi B., Gao X., Karakoc E., Li S.C., Balbach F., Feng G.,
RA Donaldson L., Li M.;
RT "Error tolerant NMR backbone resonance assignment and automated structure
RT generation.";
RL J. Bioinform. Comput. Biol. 9:15-41(2011).
CC -!- SUBUNIT: May not bind CASK.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WXE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXE0-2; Sequence=VSP_040568;
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DR EMBL; AF451976; AAL49757.1; -; mRNA.
DR EMBL; AK300354; BAG62095.1; -; mRNA.
DR EMBL; AK315936; BAH14307.1; -; mRNA.
DR EMBL; AC100787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066643; AAH66643.1; -; mRNA.
DR EMBL; AB032965; BAA86453.1; -; mRNA.
DR CCDS; CCDS11723.1; -. [Q8WXE0-1]
DR CCDS; CCDS45775.1; -. [Q8WXE0-2]
DR RefSeq; NP_001136115.1; NM_001142643.2. [Q8WXE0-2]
DR RefSeq; NP_065804.2; NM_020753.4. [Q8WXE0-1]
DR PDB; 2KE9; NMR; -; A=284-348.
DR PDB; 4IS7; X-ray; 2.75 A; A=483-633.
DR PDB; 5L1M; X-ray; 2.75 A; A=483-633.
DR PDBsum; 2KE9; -.
DR PDBsum; 4IS7; -.
DR PDBsum; 5L1M; -.
DR AlphaFoldDB; Q8WXE0; -.
DR BMRB; Q8WXE0; -.
DR SMR; Q8WXE0; -.
DR BioGRID; 121577; 44.
DR IntAct; Q8WXE0; 11.
DR MINT; Q8WXE0; -.
DR STRING; 9606.ENSP00000325355; -.
DR GlyGen; Q8WXE0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WXE0; -.
DR PhosphoSitePlus; Q8WXE0; -.
DR SwissPalm; Q8WXE0; -.
DR BioMuta; CASKIN2; -.
DR DMDM; 296434467; -.
DR EPD; Q8WXE0; -.
DR jPOST; Q8WXE0; -.
DR MassIVE; Q8WXE0; -.
DR MaxQB; Q8WXE0; -.
DR PaxDb; Q8WXE0; -.
DR PeptideAtlas; Q8WXE0; -.
DR PRIDE; Q8WXE0; -.
DR ProteomicsDB; 75016; -. [Q8WXE0-1]
DR ProteomicsDB; 75017; -. [Q8WXE0-2]
DR Antibodypedia; 53193; 168 antibodies from 26 providers.
DR DNASU; 57513; -.
DR Ensembl; ENST00000321617.8; ENSP00000325355.3; ENSG00000177303.10. [Q8WXE0-1]
DR Ensembl; ENST00000433559.6; ENSP00000406963.2; ENSG00000177303.10. [Q8WXE0-2]
DR GeneID; 57513; -.
DR KEGG; hsa:57513; -.
DR MANE-Select; ENST00000321617.8; ENSP00000325355.3; NM_020753.5; NP_065804.2.
DR UCSC; uc002joc.5; human. [Q8WXE0-1]
DR CTD; 57513; -.
DR DisGeNET; 57513; -.
DR GeneCards; CASKIN2; -.
DR HGNC; HGNC:18200; CASKIN2.
DR HPA; ENSG00000177303; Low tissue specificity.
DR MIM; 612185; gene.
DR neXtProt; NX_Q8WXE0; -.
DR OpenTargets; ENSG00000177303; -.
DR PharmGKB; PA134944093; -.
DR VEuPathDB; HostDB:ENSG00000177303; -.
DR eggNOG; KOG0507; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR GeneTree; ENSGT00940000158256; -.
DR HOGENOM; CLU_003619_2_0_1; -.
DR InParanoid; Q8WXE0; -.
DR OrthoDB; 75723at2759; -.
DR PhylomeDB; Q8WXE0; -.
DR TreeFam; TF320582; -.
DR PathwayCommons; Q8WXE0; -.
DR SignaLink; Q8WXE0; -.
DR BioGRID-ORCS; 57513; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; CASKIN2; human.
DR GenomeRNAi; 57513; -.
DR Pharos; Q8WXE0; Tdark.
DR PRO; PR:Q8WXE0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WXE0; protein.
DR Bgee; ENSG00000177303; Expressed in olfactory bulb and 178 other tissues.
DR ExpressionAtlas; Q8WXE0; baseline and differential.
DR Genevisible; Q8WXE0; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12063; SH3_Caskin2; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027013; Caskin-1/2.
DR InterPro; IPR032232; Caskin1-CID.
DR InterPro; IPR035497; Caskin1/2_SAM_1.
DR InterPro; IPR035498; Caskin1/2_SAM_2.
DR InterPro; IPR035499; Caskin2_SH3.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR24174:SF7; PTHR24174:SF7; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF16632; Caskin-tail; 1.
DR Pfam; PF16600; Caskin1-CID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1202
FT /note="Caskin-2"
FT /id="PRO_0000066983"
FT REPEAT 48..77
FT /note="ANK 1"
FT REPEAT 81..110
FT /note="ANK 2"
FT REPEAT 114..143
FT /note="ANK 3"
FT REPEAT 147..176
FT /note="ANK 4"
FT REPEAT 188..217
FT /note="ANK 5"
FT REPEAT 220..249
FT /note="ANK 6"
FT DOMAIN 281..347
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 489..552
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 558..622
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 355..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK1"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK1"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040568"
FT VARIANT 891
FT /note="E -> G (in dbSNP:rs7503373)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:12040031, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_060244"
FT CONFLICT 640
FT /note="A -> G (in Ref. 2; BAH14307)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="L -> P (in Ref. 2; BAH14307)"
FT /evidence="ECO:0000305"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:2KE9"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:2KE9"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2KE9"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2KE9"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:2KE9"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:2KE9"
FT HELIX 490..499
FT /evidence="ECO:0007829|PDB:4IS7"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:5L1M"
FT HELIX 507..512
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 525..530
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:4IS7"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 563..569
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 576..581
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:4IS7"
FT HELIX 606..624
FT /evidence="ECO:0007829|PDB:4IS7"
SQ SEQUENCE 1202 AA; 126783 MW; 881E6BAEEBDF3DC5 CRC64;
MGREQDLILA VKNGDVTGVQ KLVAKVKATK TKLLGSTKRL NVNYQDADGF SALHHAALGG
SLELIALLLE AQATVDIKDS NGMRPLHYAA WQGRLEPVRL LLRASAAVNA ASLDGQIPLH
LAAQYGHYEV SEMLLQHQSN PCLVNKAKKT PLDLACEFGR LKVAQLLLNS HLCVALLEGE
AKDPCDPNYT TPLHLAAKNG HREVIRQLLR AGIEINRQTK TGTALHEAAL YGKTEVVRLL
LEGGVDVNIR NTYNQTALDI VNQFTTSQAS REIKQLLREA SGILKVRALK DFWNLHDPTA
LNVRAGDVIT VLEQHPDGRW KGHIHESQRG TDRIGYFPPG IVEVVSKRVG IPAARLPSAP
TPLRPGFSRT PQPPAEEPPH PLTYSQLPRV GLSPDSPAGD RNSVGSEGSV GSIRSAGSGQ
SSEGTNGHGP GLLIENAQPL PSAGEDQVLP GLHPPSLADN LSHRPLANCR SGEQIFTQDV
RPEQLLEGKD AQAIHNWLSE FQLEGYTAHF LQAGYDVPTI SRMTPEDLTA IGVTKPGHRK
KIASEIAQLS IAEWLPSYIP TDLLEWLCAL GLPQYHKQLV SSGYDSMGLV ADLTWEELQE
IGVNKLGHQK KLMLGVKRLA ELRRGLLQGE ALSEGGRRLA KGPELMAIEG LENGEGPATA
GPRLLTFQGS ELSPELQAAM AGGGPEPLPL PPARSPSQES IGARSRGSGH SQEQPAPQPS
GGDPSPPQER NLPEGTERPP KLCSSLPGQG PPPYVFMYPQ GSPSSPAPGP PPGAPWAFSY
LAGPPATPPD PPRPKRRSHS LSRPGPTEGD AEGEAEGPVG STLGSYATLT RRPGRSALVR
TSPSVTPTPA RGTPRSQSFA LRARRKGPPP PPPKRLSSVS GPSPEPPPLD ESPGPKEGAT
GPRRRTLSEP AGPSEPPGPP APAGPASDTE EEEPGPEGTP PSRGSSGEGL PFAEEGNLTI
KQRPKPAGPP PRETPVPPGL DFNLTESDTV KRRPKCRERE PLQTALLAFG VASATPGPAA
PLPSPTPGES PPASSLPQPE PSSLPAQGVP TPLAPSPAMQ PPVPPCPGPG LESSAASRWN
GETEPPAAPA ALLKVPGAGT APKPVSVACT QLAFSGPKLA PRLGPRPVPP PRPESTGTVG
PGQAQQRLEQ TSSSLAAALR AAEKSIGTKE QEGTPSASTK HILDDISTMF DALADQLDAM
LD
