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   27-MAR-2024, entry version 171.
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).
RN   [12]
RP   INVOLVEMENT IN BRDCS2, AND VARIANT BRDCS2 501-ARG--SER-1388 DEL.
RX   PubMed=28150392; DOI=10.1002/humu.23188;
RA   Sleiman P.M.A., March M., Nguyen K., Tian L., Pellegrino R., Hou C.,
RA   Dridi W., Sager M., Housawi Y.H., Hakonarson H.;
RT   "Loss-of-Function Mutations in KIF15 Underlying a Braddock-Carey
RT   Genocopy.";
RL   Hum. Mutat. 38:507-510(2017).
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   -!- DISEASE: Braddock-Carey syndrome 2 (BRDCS2) [MIM:619981]: An autosomal
CC       recessive disease characterized by microcephaly, congenital
CC       thrombocytopenia, and facial dysmorphisms including Pierre-Robin
CC       sequence. {ECO:0000269|PubMed:28150392}. Note=The disease may be caused
CC       by variants affecting the gene represented in this entry.
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   EMDB; EMD-11339; -.
DR   EMDB; EMD-11340; -.
DR   EMDB; EMD-24744; -.
DR   SMR; Q9NS87; -.
DR   BioGRID; 121307; 77.
DR   DIP; DIP-28133N; -.
DR   IntAct; Q9NS87; 27.
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; 9606-ENSP00000324020; -.
DR   PeptideAtlas; Q9NS87; -.
DR   ProteomicsDB; 82511; -. [Q9NS87-1]
DR   ProteomicsDB; 82512; -. [Q9NS87-2]
DR   ProteomicsDB; 82513; -. [Q9NS87-3]
DR   ProteomicsDB; 82514; -. [Q9NS87-4]
DR   Pumba; Q9NS87; -.
DR   Antibodypedia; 29484; 226 antibodies from 26 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   AGR; HGNC:17273; -.
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   MIM; 619981; phenotype.
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; SEYNFKM; -.
DR   OrthoDB; 2915018at2759; -.
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 1159 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 103 other cell types or tissues.
DR   ExpressionAtlas; Q9NS87; baseline and differential.
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   CDD; cd01373; KISc_KLP2_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR044986; KIF15/KIN-12.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR   PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR   Pfam; PF15908; HMMR_C; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   Genevisible; Q9NS87; HS.
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         501..1388
FT                   /note="Missing (in BRDCS2; uncertain significance;
FT                   dbSNP:rs1002572191)"
FT                   /evidence="ECO:0000269|PubMed:28150392"
FT                   /id="VAR_087453"
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
//