TBC20_HUMAN
ID TBC20_HUMAN Reviewed; 403 AA.
AC Q96BZ9; A8K6I3; B9A6M1; Q5JWQ7; Q6ZSY8; Q96NE1; Q9BYM7; Q9H140;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=TBC1 domain family member 20;
GN Name=TBC1D20; Synonyms=C20orf140;
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).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Lung, and 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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [6]
RP INTERACTION WITH HCV NS5A (MICROBIAL INFECTION).
RX PubMed=17686842; DOI=10.1128/jvi.01249-07;
RA Sklan E.H., Staschke K., Oakes T.M., Elazar M., Winters M., Aroeti B.,
RA Danieli T., Glenn J.S.;
RT "A Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates
RT viral replication.";
RL J. Virol. 81:11096-11105(2007).
RN [7]
RP INVOLVEMENT IN WARBM4.
RX PubMed=24239381; DOI=10.1016/j.ajhg.2013.10.011;
RA Liegel R.P., Handley M.T., Ronchetti A., Brown S., Langemeyer L.,
RA Linford A., Chang B., Morris-Rosendahl D.J., Carpanini S., Posmyk R.,
RA Harthill V., Sheridan E., Abdel-Salam G.M., Terhal P.A., Faravelli F.,
RA Accorsi P., Giordano L., Pinelli L., Hartmann B., Ebert A.D., Barr F.A.,
RA Aligianis I.A., Sidjanin D.J.;
RT "Loss-of-function mutations in TBC1D20 cause cataracts and male infertility
RT in blind sterile mice and Warburg micro syndrome in humans.";
RL Am. J. Hum. Genet. 93:1001-1014(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 14-305 ALONE AND IN COMPLEX WITH
RP RAB1B, MUTAGENESIS OF ARG-105 AND GLN-144, AND ARGININE AND GLUTAMINE
RP FINGERS.
RX PubMed=23236136; DOI=10.1073/pnas.1214431110;
RA Gavriljuk K., Gazdag E.M., Itzen A., Kotting C., Goody R.S., Gerwert K.;
RT "Catalytic mechanism of a mammalian Rab.RabGAP complex in atomic detail.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21348-21353(2012).
CC -!- FUNCTION: GTPase-activating protein specific for Rab1 and Rab2 small
CC GTPase families for which it can accelerate the intrinsic GTP
CC hydrolysis rate by more than five orders of magnitude.
CC -!- SUBUNIT: (Microbial infection) Directly interacts with the N-terminal
CC amphipathic helix of hepatitis C virus (HCV) NS5A.
CC {ECO:0000269|PubMed:17686842}.
CC -!- INTERACTION:
CC Q96BZ9; P55056: APOC4; NbExp=3; IntAct=EBI-9254454, EBI-18302142;
CC Q96BZ9; Q13520: AQP6; NbExp=3; IntAct=EBI-9254454, EBI-13059134;
CC Q96BZ9; Q15125: EBP; NbExp=3; IntAct=EBI-9254454, EBI-3915253;
CC Q96BZ9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-9254454, EBI-8638294;
CC Q96BZ9; PRO_0000037576 [P27958]; Xeno; NbExp=11; IntAct=EBI-9254454, EBI-8753518;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96BZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BZ9-2; Sequence=VSP_008100, VSP_008101, VSP_008102;
CC Name=3;
CC IsoId=Q96BZ9-3; Sequence=VSP_031524;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000269|PubMed:23236136}.
CC -!- DISEASE: Warburg micro syndrome 4 (WARBM4) [MIM:615663]: A form of
CC Warburg micro syndrome, a rare syndrome characterized by microcephaly,
CC microphthalmia, microcornia, congenital cataracts, optic atrophy,
CC cortical dysplasia, in particular corpus callosum hypoplasia, severe
CC intellectual disability, spastic diplegia, and hypogonadism.
CC {ECO:0000269|PubMed:24239381}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AB449906; BAH16649.1; -; mRNA.
DR EMBL; AK055573; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127062; BAC86808.1; -; mRNA.
DR EMBL; AK291648; BAF84337.1; -; mRNA.
DR EMBL; AL049761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10670.1; -; Genomic_DNA.
DR EMBL; BC014983; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13002.1; -. [Q96BZ9-1]
DR RefSeq; NP_653229.1; NM_144628.3. [Q96BZ9-1]
DR RefSeq; XP_005260718.1; XM_005260661.1. [Q96BZ9-1]
DR PDB; 4HL4; X-ray; 2.20 A; A=14-305.
DR PDB; 4HLQ; X-ray; 3.30 A; A/C/E/G/I=1-305.
DR PDBsum; 4HL4; -.
DR PDBsum; 4HLQ; -.
DR AlphaFoldDB; Q96BZ9; -.
DR SMR; Q96BZ9; -.
DR BioGRID; 126139; 24.
DR IntAct; Q96BZ9; 9.
DR MINT; Q96BZ9; -.
DR STRING; 9606.ENSP00000346139; -.
DR iPTMnet; Q96BZ9; -.
DR MetOSite; Q96BZ9; -.
DR PhosphoSitePlus; Q96BZ9; -.
DR BioMuta; TBC1D20; -.
DR DMDM; 34395569; -.
DR EPD; Q96BZ9; -.
DR jPOST; Q96BZ9; -.
DR MassIVE; Q96BZ9; -.
DR MaxQB; Q96BZ9; -.
DR PaxDb; Q96BZ9; -.
DR PeptideAtlas; Q96BZ9; -.
DR PRIDE; Q96BZ9; -.
DR ProteomicsDB; 76134; -. [Q96BZ9-1]
DR ProteomicsDB; 76136; -. [Q96BZ9-3]
DR Antibodypedia; 22961; 109 antibodies from 20 providers.
DR DNASU; 128637; -.
DR Ensembl; ENST00000354200.5; ENSP00000346139.4; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000461304.5; ENSP00000432280.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000679741.1; ENSP00000504904.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000679944.1; ENSP00000506278.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000680106.1; ENSP00000505500.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000680284.1; ENSP00000506231.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000680792.1; ENSP00000506012.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000681539.1; ENSP00000505557.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000681636.1; ENSP00000506155.1; ENSG00000125875.15. [Q96BZ9-1]
DR Ensembl; ENST00000681742.1; ENSP00000506122.1; ENSG00000125875.15. [Q96BZ9-1]
DR GeneID; 128637; -.
DR KEGG; hsa:128637; -.
DR MANE-Select; ENST00000354200.5; ENSP00000346139.4; NM_144628.4; NP_653229.1.
DR UCSC; uc002wds.4; human. [Q96BZ9-1]
DR CTD; 128637; -.
DR DisGeNET; 128637; -.
DR GeneCards; TBC1D20; -.
DR GeneReviews; TBC1D20; -.
DR HGNC; HGNC:16133; TBC1D20.
DR HPA; ENSG00000125875; Low tissue specificity.
DR MalaCards; TBC1D20; -.
DR MIM; 611663; gene.
DR MIM; 615663; phenotype.
DR neXtProt; NX_Q96BZ9; -.
DR OpenTargets; ENSG00000125875; -.
DR Orphanet; 2510; Micro syndrome.
DR PharmGKB; PA25683; -.
DR VEuPathDB; HostDB:ENSG00000125875; -.
DR eggNOG; KOG2595; Eukaryota.
DR GeneTree; ENSGT00390000014944; -.
DR HOGENOM; CLU_039465_1_0_1; -.
DR InParanoid; Q96BZ9; -.
DR OMA; YPMLCYF; -.
DR PhylomeDB; Q96BZ9; -.
DR TreeFam; TF105942; -.
DR PathwayCommons; Q96BZ9; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SABIO-RK; Q96BZ9; -.
DR SignaLink; Q96BZ9; -.
DR BioGRID-ORCS; 128637; 57 hits in 1081 CRISPR screens.
DR ChiTaRS; TBC1D20; human.
DR GenomeRNAi; 128637; -.
DR Pharos; Q96BZ9; Tbio.
DR PRO; PR:Q96BZ9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96BZ9; protein.
DR Bgee; ENSG00000125875; Expressed in tendon of biceps brachii and 181 other tissues.
DR Genevisible; Q96BZ9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0070309; P:lens fiber cell morphogenesis; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; IEA:Ensembl.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IMP:AgBase.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0019068; P:virion assembly; IMP:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR045913; TBC20/Gyp8-like.
DR PANTHER; PTHR20913; PTHR20913; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation;
KW Host-virus interaction; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="TBC1 domain family member 20"
FT /id="PRO_0000208048"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 60..246
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 105
FT /note="Arginine finger"
FT /evidence="ECO:0000269|PubMed:23236136"
FT SITE 144
FT /note="Glutamine finger"
FT /evidence="ECO:0000269|PubMed:23236136"
FT VAR_SEQ 1..192
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008100"
FT VAR_SEQ 1
FT /note="M -> MPSGCYVPRSEPRLLPAPPPAGARVG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031524"
FT VAR_SEQ 209..364
FT /note="SAEVGTIFALSWLITWFGHVLSDFRHVVRLYDFFLACHPLMPIYFAAVIVLY
FT REQEVLDCDCDMASVHHLLSQIPQDLPYETLISRAGDLFVQFPPSELAREAAAQQQAER
FT TAASTFKDFELASAQQRPDMVLRQRFRGLLRPEDRTKDVLTKPRT -> RYICVCISVC
FT MHTHAHTPPHLKHSSQAERSFLIVLGGFVKFSPVVPVTSNLGNSVLGAFLGTVLFGGHS
FT PSLEFTSSGERWIRYVCQGKMLRLLPQEKHKVLWDPVARRGRPTMGCFISQVPKRRNIF
FT LQIPCDVLFLLCLVGNVFLANASFFKIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008101"
FT VAR_SEQ 365..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008102"
FT VARIANT 79
FT /note="N -> S (in dbSNP:rs36088178)"
FT /id="VAR_052543"
FT MUTAGEN 105
FT /note="R->A: 1000-fold decrease in GAP activity."
FT /evidence="ECO:0000269|PubMed:23236136"
FT MUTAGEN 144
FT /note="Q->L: 1000-fold decrease in GAP activity."
FT /evidence="ECO:0000269|PubMed:23236136"
FT CONFLICT 117
FT /note="E -> G (in Ref. 2; BAC86808)"
FT /evidence="ECO:0000305"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:4HL4"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:4HL4"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:4HLQ"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:4HL4"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4HLQ"
FT HELIX 116..136
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:4HL4"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4HL4"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4HL4"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:4HL4"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:4HL4"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:4HL4"
SQ SEQUENCE 403 AA; 45855 MW; 70B011A33DEF527D CRC64;
MALRSAQGDG PTSGHWDGGA EKADFNAKRK KKVAEIHQAL NSDPTDVAAL RRMAISEGGL
LTDEIRRKVW PKLLNVNAND PPPISGKNLR QMSKDYQQVL LDVRRSLRRF PPGMPEEQRE
GLQEELIDII LLILERNPQL HYYQGYHDIV VTFLLVVGER LATSLVEKLS THHLRDFMDP
TMDNTKHILN YLMPIIDQVN PELHDFMQSA EVGTIFALSW LITWFGHVLS DFRHVVRLYD
FFLACHPLMP IYFAAVIVLY REQEVLDCDC DMASVHHLLS QIPQDLPYET LISRAGDLFV
QFPPSELARE AAAQQQAERT AASTFKDFEL ASAQQRPDMV LRQRFRGLLR PEDRTKDVLT
KPRTNRFVKL AVMGLTVALG AAALAVVKSA LEWAPKFQLQ LFP
