KATL1_HUMAN
ID KATL1_HUMAN Reviewed; 490 AA.
AC Q9BW62; A8K5X4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE Short=Katanin p60 subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE AltName: Full=p60 katanin-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
GN Name=KATNAL1 {ECO:0000255|HAMAP-Rule:MF_03024};
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22654668; DOI=10.1371/journal.pgen.1002697;
RA Smith L.B., Milne L., Nelson N., Eddie S., Brown P., Atanassova N.,
RA O'Bryan M.K., O'Donnell L., Rhodes D., Wells S., Napper D., Nolan P.,
RA Lalanne Z., Cheeseman M., Peters J.;
RT "KATNAL1 regulation of Sertoli cell microtubule dynamics is essential for
RT spermiogenesis and male fertility.";
RL PLoS Genet. 8:E1002697-E1002697(2012).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, INTERACTION WITH KATNB1 AND KATNBL1, AND SUBCELLULAR LOCATION.
RX PubMed=26929214; DOI=10.1074/mcp.m115.056465;
RA Cheung K., Senese S., Kuang J., Bui N., Ongpipattanakul C., Gholkar A.,
RA Cohn W., Capri J., Whitelegge J.P., Torres J.Z.;
RT "Proteomic analysis of the mammalian Katanin family of microtubule-severing
RT enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of
RT mammalian Katanin microtubule-severing.";
RL Mol. Cell. Proteomics 15:1658-1669(2016).
CC -!- FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process
CC that is essential for spermiogenesis and male fertility. Severs
CC microtubules in an ATP-dependent manner, promoting rapid reorganization
CC of cellular microtubule arrays (By similarity). Has microtubule-
CC severing activity in vitro (PubMed:26929214).
CC {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000269|PubMed:26929214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03024};
CC -!- SUBUNIT: Interacts with KATNB1 and KATNBL1.
CC {ECO:0000269|PubMed:26929214}.
CC -!- INTERACTION:
CC Q9BW62; Q9H1I8: ASCC2; NbExp=3; IntAct=EBI-743591, EBI-711197;
CC Q9BW62; Q13895: BYSL; NbExp=3; IntAct=EBI-743591, EBI-358049;
CC Q9BW62; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-743591, EBI-8643161;
CC Q9BW62; Q8IYX8: CEP57L1; NbExp=9; IntAct=EBI-743591, EBI-1104570;
CC Q9BW62; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-743591, EBI-10181988;
CC Q9BW62; Q14061: COX17; NbExp=4; IntAct=EBI-743591, EBI-711311;
CC Q9BW62; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-743591, EBI-11962928;
CC Q9BW62; Q96CN9: GCC1; NbExp=3; IntAct=EBI-743591, EBI-746252;
CC Q9BW62; P43080: GUCA1A; NbExp=3; IntAct=EBI-743591, EBI-6873005;
CC Q9BW62; Q8NA54: IQUB; NbExp=3; IntAct=EBI-743591, EBI-10220600;
CC Q9BW62; Q9BW62: KATNAL1; NbExp=4; IntAct=EBI-743591, EBI-743591;
CC Q9BW62; Q9BVA0: KATNB1; NbExp=8; IntAct=EBI-743591, EBI-11147603;
CC Q9BW62; Q9H079: KATNBL1; NbExp=19; IntAct=EBI-743591, EBI-715394;
CC Q9BW62; Q9NSK0: KLC4; NbExp=6; IntAct=EBI-743591, EBI-949319;
CC Q9BW62; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-743591, EBI-16439278;
CC Q9BW62; P15259: PGAM2; NbExp=3; IntAct=EBI-743591, EBI-2511669;
CC Q9BW62; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-743591, EBI-14223623;
CC Q9BW62; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-743591, EBI-747107;
CC Q9BW62; O75351: VPS4B; NbExp=3; IntAct=EBI-743591, EBI-2514459;
CC Q9BW62; Q9UC07: ZNF69; NbExp=3; IntAct=EBI-743591, EBI-10320266;
CC Q9BW62; Q9UC07-2: ZNF69; NbExp=6; IntAct=EBI-743591, EBI-12310821;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03024, ECO:0000269|PubMed:22654668}. Cytoplasm
CC {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:26929214}. Note=Colocalizes with microtubules
CC throughout the basal and adluminal compartments of Sertoli cells (By
CC similarity). Localizes within the cytoplasm, partially overlapping with
CC microtubules, in interphase and to the mitotic spindle and spindle
CC poles during mitosis (PubMed:26929214). {ECO:0000250|UniProtKB:Q8K0T4,
CC ECO:0000269|PubMed:26929214}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, restricted to Sertoli cells
CC (at protein level). {ECO:0000269|PubMed:22654668}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 1 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03024}.
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DR EMBL; AK291439; BAF84128.1; -; mRNA.
DR EMBL; AL356750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08452.1; -; Genomic_DNA.
DR EMBL; BC000612; AAH00612.1; -; mRNA.
DR CCDS; CCDS31956.1; -.
DR RefSeq; NP_001014402.1; NM_001014380.2.
DR RefSeq; NP_115492.1; NM_032116.4.
DR RefSeq; XP_005266631.1; XM_005266574.2.
DR PDB; 6B5C; X-ray; 2.40 A; A=184-490.
DR PDBsum; 6B5C; -.
DR AlphaFoldDB; Q9BW62; -.
DR SMR; Q9BW62; -.
DR BioGRID; 123851; 35.
DR ComplexPortal; CPX-6381; Katanin complex, KATNAL1-KATNBL1 variant.
DR ComplexPortal; CPX-6382; Katanin complex, KATNAL1-KATNB1 variant.
DR CORUM; Q9BW62; -.
DR IntAct; Q9BW62; 48.
DR STRING; 9606.ENSP00000369989; -.
DR iPTMnet; Q9BW62; -.
DR PhosphoSitePlus; Q9BW62; -.
DR BioMuta; KATNAL1; -.
DR DMDM; 60390214; -.
DR EPD; Q9BW62; -.
DR jPOST; Q9BW62; -.
DR MassIVE; Q9BW62; -.
DR MaxQB; Q9BW62; -.
DR PaxDb; Q9BW62; -.
DR PeptideAtlas; Q9BW62; -.
DR PRIDE; Q9BW62; -.
DR ProteomicsDB; 79256; -.
DR Antibodypedia; 49047; 198 antibodies from 20 providers.
DR DNASU; 84056; -.
DR Ensembl; ENST00000380615.8; ENSP00000369989.3; ENSG00000102781.14.
DR Ensembl; ENST00000380617.7; ENSP00000369991.3; ENSG00000102781.14.
DR GeneID; 84056; -.
DR KEGG; hsa:84056; -.
DR MANE-Select; ENST00000380615.8; ENSP00000369989.3; NM_032116.5; NP_115492.1.
DR UCSC; uc001uss.5; human.
DR CTD; 84056; -.
DR DisGeNET; 84056; -.
DR GeneCards; KATNAL1; -.
DR HGNC; HGNC:28361; KATNAL1.
DR HPA; ENSG00000102781; Low tissue specificity.
DR MIM; 614764; gene.
DR neXtProt; NX_Q9BW62; -.
DR OpenTargets; ENSG00000102781; -.
DR PharmGKB; PA134951885; -.
DR VEuPathDB; HostDB:ENSG00000102781; -.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q9BW62; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q9BW62; -.
DR TreeFam; TF323170; -.
DR BRENDA; 5.6.1.1; 2681.
DR PathwayCommons; Q9BW62; -.
DR SignaLink; Q9BW62; -.
DR BioGRID-ORCS; 84056; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; KATNAL1; human.
DR GenomeRNAi; 84056; -.
DR Pharos; Q9BW62; Tbio.
DR PRO; PR:Q9BW62; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9BW62; protein.
DR Bgee; ENSG00000102781; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q9BW62; baseline and differential.
DR Genevisible; Q9BW62; HS.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0008352; C:katanin complex; IPI:ComplexPortal.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IC:ComplexPortal.
DR GO; GO:0051013; P:microtubule severing; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR HAMAP; MF_03024; Katanin_p60_AL1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR028594; Katnal1_chordates.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..490
FT /note="Katanin p60 ATPase-containing subunit A-like 1"
FT /id="PRO_0000084601"
FT REGION 95..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK7"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 319..338
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:6B5C"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:6B5C"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 417..438
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 441..446
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:6B5C"
FT HELIX 474..487
FT /evidence="ECO:0007829|PDB:6B5C"
SQ SEQUENCE 490 AA; 55392 MW; CB8E51A77E5CB487 CRC64;
MNLAEICDNA KKGREYALLG NYDSSMVYYQ GVMQQIQRHC QSVRDPAIKG KWQQVRQELL
EEYEQVKSIV STLESFKIDK PPDFPVSCQD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
RPLRKEMAGV GARGPVGRAH PISKSEKPST SRDKDYRARG RDDKGRKNMQ DGASDGEMPK
FDGAGYDKDL VEALERDIVS RNPSIHWDDI ADLEEAKKLL REAVVLPMWM PDFFKGIRRP
WKGVLMVGPP GTGKTMLAKA VATECGTTFF NVSSSTLTSK YRGESEKLVR LLFEMARFYA
PTTIFIDEID SICSRRGTSD EHEASRRVKS ELLIQMDGVG GALENDDPSK MVMVLAATNF
PWDIDEALRR RLEKRIYIPL PTAKGRAELL KINLREVELD PDIQLEDIAE KIEGYSGADI
TNVCRDASLM AMRRRINGLS PEEIRALSKE ELQMPVTKGD FELALKKIAK SVSAADLEKY
EKWMVEFGSA
