KIF15_HUMAN
ID KIF15_HUMAN Reviewed; 1388 AA.
AC Q9NS87; Q17RV9; Q69YL6; Q96JX7; Q9H280;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Kinesin-like protein KIF15;
DE AltName: Full=Kinesin-like protein 2;
DE Short=hKLP2;
DE AltName: Full=Kinesin-like protein 7;
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-62;
GN Name=KIF15; Synonyms=KLP2, KNSL7;
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), INTERACTION WITH MKI67, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10878014; DOI=10.1074/jbc.m003879200;
RA Sueishi M., Takagi M., Yoneda Y.;
RT "The forkhead-associated domain of Ki-67 antigen interacts with the novel
RT kinesin-like protein Hklp2.";
RL J. Biol. Chem. 275:28888-28892(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [LARGE SCALE MRNA] OF 339-1388 (ISOFORMS 1/2), AND
RP VARIANT SER-996.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 786-1388 (ISOFORM 4), TISSUE SPECIFICITY, AND
RP VARIANT SER-996.
RC TISSUE=Mammary gland;
RX PubMed=12747765;
RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT "Humoral immunity to human breast cancer: antigen definition and
RT quantitative analysis of mRNA expression.";
RL Cancer Immun. 1:4-4(2001).
RN [6]
RP INTERACTION WITH TPX2, AND SUBCELLULAR LOCATION.
RX PubMed=12612055;
RA Heidebrecht H.-J., Adam-Klages S., Szczepanowski M., Pollmann M., Buck F.,
RA Endl E., Kruse M.-L., Rudolph P., Parwaresch R.;
RT "repp86: a human protein associated in the progression of mitosis.";
RL Mol. Cancer Res. 1:271-279(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568, AND IDENTIFICATION BY
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1009, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1169, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399 AND SER-1141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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).
CC -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC mitotic spindle assembly. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MKI67 and TPX2. {ECO:0000269|PubMed:10878014,
CC ECO:0000269|PubMed:12612055}.
CC -!- INTERACTION:
CC Q9NS87; P46013: MKI67; NbExp=3; IntAct=EBI-712159, EBI-876367;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC Note=Detected during the interphase in the cytoplasm as finely
CC punctuate pattern and irregularly shaped dots. Detected during mitosis
CC on the mitotic spindle. Colocalizes with TPX2 in mitosis. Localizes at
CC the central spindle at anaphase (By similarity). Localizes at the sites
CC of invaginating cell membranes, a position that corresponds to the
CC location of the contractile actomyosin ring of dividing cells (By
CC similarity). Colocalizes with actin in interphase (By similarity).
CC Colocalizes in dendrites and in growth cone of axons with microtubules
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NS87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NS87-2; Sequence=VSP_032753;
CC Name=3;
CC IsoId=Q9NS87-3; Sequence=VSP_032752;
CC Name=4;
CC IsoId=Q9NS87-4; Sequence=VSP_032754, VSP_032755;
CC -!- TISSUE SPECIFICITY: Expressed in testis, colon, thymus and in breast
CC cancer. {ECO:0000269|PubMed:12747765}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KLP2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG48261.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB035898; BAB03309.1; -; mRNA.
DR EMBL; AK027816; BAB55389.1; -; mRNA.
DR EMBL; BC117174; AAI17175.1; -; mRNA.
DR EMBL; AL832908; CAH10635.1; -; mRNA.
DR EMBL; AF308294; AAG48261.1; ALT_FRAME; mRNA.
DR CCDS; CCDS33744.1; -. [Q9NS87-1]
DR RefSeq; NP_064627.1; NM_020242.2. [Q9NS87-1]
DR PDB; 4BN2; X-ray; 2.70 A; A/B/C=19-375.
DR PDB; 6ZPH; EM; 6.90 A; B=1-374.
DR PDB; 6ZPI; EM; 4.50 A; C=1-374.
DR PDB; 7RYP; EM; 4.80 A; A=1-375.
DR PDBsum; 4BN2; -.
DR PDBsum; 6ZPH; -.
DR PDBsum; 6ZPI; -.
DR PDBsum; 7RYP; -.
DR AlphaFoldDB; Q9NS87; -.
DR SMR; Q9NS87; -.
DR BioGRID; 121307; 65.
DR DIP; DIP-28133N; -.
DR IntAct; Q9NS87; 25.
DR MINT; Q9NS87; -.
DR STRING; 9606.ENSP00000324020; -.
DR BindingDB; Q9NS87; -.
DR ChEMBL; CHEMBL3632454; -.
DR CarbonylDB; Q9NS87; -.
DR GlyGen; Q9NS87; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NS87; -.
DR MetOSite; Q9NS87; -.
DR PhosphoSitePlus; Q9NS87; -.
DR BioMuta; KIF15; -.
DR DMDM; 74752937; -.
DR EPD; Q9NS87; -.
DR jPOST; Q9NS87; -.
DR MassIVE; Q9NS87; -.
DR MaxQB; Q9NS87; -.
DR PaxDb; Q9NS87; -.
DR PeptideAtlas; Q9NS87; -.
DR PRIDE; Q9NS87; -.
DR ProteomicsDB; 82511; -. [Q9NS87-1]
DR ProteomicsDB; 82512; -. [Q9NS87-2]
DR ProteomicsDB; 82513; -. [Q9NS87-3]
DR ProteomicsDB; 82514; -. [Q9NS87-4]
DR Antibodypedia; 29484; 205 antibodies from 25 providers.
DR DNASU; 56992; -.
DR Ensembl; ENST00000326047.9; ENSP00000324020.4; ENSG00000163808.17. [Q9NS87-1]
DR Ensembl; ENST00000627272.3; ENSP00000486004.1; ENSG00000280610.3. [Q9NS87-1]
DR GeneID; 56992; -.
DR KEGG; hsa:56992; -.
DR MANE-Select; ENST00000326047.9; ENSP00000324020.4; NM_020242.3; NP_064627.1.
DR UCSC; uc003cnx.5; human. [Q9NS87-1]
DR CTD; 56992; -.
DR DisGeNET; 56992; -.
DR GeneCards; KIF15; -.
DR HGNC; HGNC:17273; KIF15.
DR HPA; ENSG00000163808; Group enriched (bone marrow, lymphoid tissue, testis).
DR MalaCards; KIF15; -.
DR MIM; 617569; gene.
DR neXtProt; NX_Q9NS87; -.
DR OpenTargets; ENSG00000163808; -.
DR Orphanet; 261323; 21q22.11q22.12 microdeletion syndrome.
DR PharmGKB; PA30183; -.
DR VEuPathDB; HostDB:ENSG00000163808; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156463; -.
DR HOGENOM; CLU_005295_0_0_1; -.
DR InParanoid; Q9NS87; -.
DR OMA; AIRVFIR; -.
DR OrthoDB; 38542at2759; -.
DR PhylomeDB; Q9NS87; -.
DR TreeFam; TF320478; -.
DR PathwayCommons; Q9NS87; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9NS87; -.
DR BioGRID-ORCS; 56992; 61 hits in 1081 CRISPR screens.
DR ChiTaRS; KIF15; human.
DR GeneWiki; KIF15; -.
DR GenomeRNAi; 56992; -.
DR Pharos; Q9NS87; Tchem.
DR PRO; PR:Q9NS87; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NS87; protein.
DR Bgee; ENSG00000163808; Expressed in ventricular zone and 101 other tissues.
DR ExpressionAtlas; Q9NS87; baseline and differential.
DR Genevisible; Q9NS87; HS.
DR GO; GO:0005813; C:centrosome; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005873; C:plus-end kinesin complex; TAS:ProtInc.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR044986; KIF15/KIN-12E.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR37739; PTHR37739; 1.
DR Pfam; PF15908; HMMR_C; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1388
FT /note="Kinesin-like protein KIF15"
FT /id="PRO_0000328684"
FT DOMAIN 26..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..1388
FT /evidence="ECO:0000255"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1009
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..952
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032752"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032753"
FT VAR_SEQ 1092..1119
FT /note="ELTKKEALIQELQHKLNQKKEEVEQKKN -> RTDQERSPDSGTSAQAKPKE
FT RGSRTEEE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12747765"
FT /id="VSP_032754"
FT VAR_SEQ 1200..1388
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12747765"
FT /id="VSP_032755"
FT VARIANT 211
FT /note="A -> V (in dbSNP:rs34862960)"
FT /id="VAR_042464"
FT VARIANT 996
FT /note="T -> S (in dbSNP:rs11710339)"
FT /evidence="ECO:0000269|PubMed:12747765,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_042465"
FT VARIANT 1206
FT /note="L -> M (in dbSNP:rs3804583)"
FT /id="VAR_042466"
FT VARIANT 1272
FT /note="E -> D (in dbSNP:rs17076986)"
FT /id="VAR_042467"
FT CONFLICT 1057
FT /note="E -> K (in Ref. 5; AAG48261)"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 158..172
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 236..250
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 253..265
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4BN2"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4BN2"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:4BN2"
SQ SEQUENCE 1388 AA; 160160 MW; E127EB4B991CA83A CRC64;
MAPGCKTELR SVTNGQSNQP SNEGDAIKVF VRIRPPAERS GSADGEQNLC LSVLSSTSLR
LHSNPEPKTF TFDHVADVDT TQESVFATVA KSIVESCMSG YNGTIFAYGQ TGSGKTFTMM
GPSESDNFSH NLRGVIPRSF EYLFSLIDRE KEKAGAGKSF LCKCSFIEIY NEQIYDLLDS
ASAGLYLREH IKKGVFVVGA VEQVVTSAAE AYQVLSGGWR NRRVASTSMN RESSRSHAVF
TITIESMEKS NEIVNIRTSL LNLVDLAGSE RQKDTHAEGM RLKEAGNINR SLSCLGQVIT
ALVDVGNGKQ RHVCYRDSKL TFLLRDSLGG NAKTAIIANV HPGSRCFGET LSTLNFAQRA
KLIKNKAVVN EDTQGNVSQL QAEVKRLKEQ LAELASGQTP PESFLTRDKK KTNYMEYFQE
AMLFFKKSEQ EKKSLIEKVT QLEDLTLKKE KFIQSNKMIV KFREDQIIRL EKLHKESRGG
FLPEEQDRLL SELRNEIQTL REQIEHHPRV AKYAMENHSL REENRRLRLL EPVKRAQEMD
AQTIAKLEKA FSEISGMEKS DKNQQGFSPK AQKEPCLFAN TEKLKAQLLQ IQTELNNSKQ
EYEEFKELTR KRQLELESEL QSLQKANLNL ENLLEATKAC KRQEVSQLNK IHAETLKIIT
TPTKAYQLHS RPVPKLSPEM GSFGSLYTQN SSILDNDILN EPVPPEMNEQ AFEAISEELR
TVQEQMSALQ AKLDEEEHKN LKLQQHVDKL EHHSTQMQEL FSSERIDWTK QQEELLSQLN
VLEKQLQETQ TKNDFLKSEV HDLRVVLHSA DKELSSVKLE YSSFKTNQEK EFNKLSERHM
HVQLQLDNLR LENEKLLESK ACLQDSYDNL QEIMKFEIDQ LSRNLQNFKK ENETLKSDLN
NLMELLEAEK ERNNKLSLQF EEDKENSSKE ILKVLEAVRQ EKQKETAKCE QQMAKVQKLE
ESLLATEKVI SSLEKSRDSD KKVVADLMNQ IQELRTSVCE KTETIDTLKQ ELKDINCKYN
SALVDREESR VLIKKQEVDI LDLKETLRLR ILSEDIERDM LCEDLAHATE QLNMLTEASK
KHSGLLQSAQ EELTKKEALI QELQHKLNQK KEEVEQKKNE YNFKMRQLEH VMDSAAEDPQ
SPKTPPHFQT HLAKLLETQE QEIEDGRASK TSLEHLVTKL NEDREVKNAE ILRMKEQLRE
MENLRLESQQ LIEKNWLLQG QLDDIKRQKE NSDQNHPDNQ QLKNEQEESI KERLAKSKIV
EEMLKMKADL EEVQSALYNK EMECLRMTDE VERTQTLESK AFQEKEQLRS KLEEMYEERE
RTSQEMEMLR KQVECLAEEN GKLVGHQNLH QKIQYVVRLK KENVRLAEET EKLRAENVFL
KEKKRSES
