RASEF_HUMAN
ID RASEF_HUMAN Reviewed; 740 AA.
AC Q8IZ41; A6NC29; Q96N04;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ras and EF-hand domain-containing protein;
DE AltName: Full=Ras-related protein Rab-45;
GN Name=RASEF; Synonyms=RAB45;
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] (ISOFORM 2).
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 TISSUE SPECIFICITY.
RX PubMed=16174859; DOI=10.1093/jnci/dji280;
RA Joensson G., Bendahl P.O., Sandberg T., Kurbasic A., Staaf J., Sunde L.,
RA Crueger D.G., Ingvar C., Olsson H., Borg A.;
RT "Mapping of a novel ocular and cutaneous malignant melanoma susceptibility
RT locus to chromosome 9q21.32.";
RL J. Natl. Cancer Inst. 97:1377-1382(2005).
RN [6]
RP SUBUNIT, FUNCTION, MUTAGENESIS OF SER-555 AND GLN-600, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17448446; DOI=10.1016/j.bbrc.2007.03.206;
RA Shintani M., Tada M., Kobayashi T., Kajiho H., Kontani K., Katada T.;
RT "Characterization of Rab45/RASEF containing EF-hand domain and a coiled-
RT coil motif as a self-associating GTPase.";
RL Biochem. Biophys. Res. Commun. 357:661-667(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH THE DYNEIN-DYNACTIN COMPLEX.
RX PubMed=30814157; DOI=10.1083/jcb.201806097;
RA Wang Y., Huynh W., Skokan T.D., Lu W., Weiss A., Vale R.D.;
RT "CRACR2a is a calcium-activated dynein adaptor protein that regulates
RT endocytic traffic.";
RL J. Cell Biol. 218:1619-1633(2019).
RN [8] {ECO:0007744|PDB:2P5S}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 533-712 IN COMPLEX WITH GDP.
RA Zhu H., Wang J., Shen Y., Tempel W., Landry R., Arrowsmith C.H.,
RA Edwards A.M., Sundstrom M., Weigelt J., Bochkarev A., Park H.;
RT "RAB domain of human RASEF in complex with GDP.";
RL Submitted (MAR-2007) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-75 IN COMPLEX WITH CALCIUM IONS.
RG Structural genomics consortium (SGC);
RT "EF-hand domain of human RASEF.";
RL Submitted (MAY-2007) to the PDB data bank.
RN [10]
RP VARIANT CYS-262.
RX PubMed=16015647; DOI=10.1002/gcc.20236;
RA Sweetser D.A., Peniket A.J., Haaland C., Blomberg A.A., Zhang Y.,
RA Zaidi S.T., Dayyani F., Zhao Z., Heerema N.A., Boultwood J., Dewald G.W.,
RA Paietta E., Slovak M.L., Willman C.L., Wainscoat J.S., Bernstein I.D.,
RA Daly S.B.;
RT "Delineation of the minimal commonly deleted segment and identification of
RT candidate tumor-suppressor genes in del(9q) acute myeloid leukemia.";
RL Genes Chromosomes Cancer 44:279-291(2005).
CC -!- FUNCTION: Binds predominantly GDP, and also GTP (PubMed:17448446). Acts
CC as a dynein adapter protein that activates dynein-mediated transport
CC and dynein-dynactin motility on microtubules (PubMed:30814157).
CC {ECO:0000269|PubMed:17448446, ECO:0000269|PubMed:30814157}.
CC -!- SUBUNIT: Homodimer (PubMed:17448446). Interacts with the dynein-
CC dynactin complex (PubMed:30814157). {ECO:0000269|PubMed:17448446,
CC ECO:0000269|PubMed:30814157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17448446}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZ41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ41-2; Sequence=VSP_027766, VSP_027767;
CC -!- TISSUE SPECIFICITY: Down-regulated in cutaneous melanoma cells but not
CC in breast cancer cells. {ECO:0000269|PubMed:16174859}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK056176; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL499602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62643.1; -; Genomic_DNA.
DR EMBL; BC023566; AAH23566.1; -; mRNA.
DR CCDS; CCDS6662.1; -. [Q8IZ41-1]
DR RefSeq; NP_689786.2; NM_152573.3. [Q8IZ41-1]
DR PDB; 2P5S; X-ray; 2.15 A; A/B=533-712.
DR PDB; 2PMY; X-ray; 2.30 A; A/B=3-75.
DR PDBsum; 2P5S; -.
DR PDBsum; 2PMY; -.
DR AlphaFoldDB; Q8IZ41; -.
DR SMR; Q8IZ41; -.
DR BioGRID; 127651; 26.
DR IntAct; Q8IZ41; 4.
DR STRING; 9606.ENSP00000365630; -.
DR iPTMnet; Q8IZ41; -.
DR PhosphoSitePlus; Q8IZ41; -.
DR BioMuta; RASEF; -.
DR DMDM; 74750780; -.
DR EPD; Q8IZ41; -.
DR jPOST; Q8IZ41; -.
DR MassIVE; Q8IZ41; -.
DR MaxQB; Q8IZ41; -.
DR PaxDb; Q8IZ41; -.
DR PeptideAtlas; Q8IZ41; -.
DR PRIDE; Q8IZ41; -.
DR ProteomicsDB; 71277; -. [Q8IZ41-1]
DR ProteomicsDB; 71278; -. [Q8IZ41-2]
DR TopDownProteomics; Q8IZ41-2; -. [Q8IZ41-2]
DR Antibodypedia; 13004; 103 antibodies from 25 providers.
DR DNASU; 158158; -.
DR Ensembl; ENST00000340717.4; ENSP00000345651.4; ENSG00000165105.10. [Q8IZ41-2]
DR Ensembl; ENST00000376447.4; ENSP00000365630.3; ENSG00000165105.10. [Q8IZ41-1]
DR GeneID; 158158; -.
DR KEGG; hsa:158158; -.
DR MANE-Select; ENST00000376447.4; ENSP00000365630.3; NM_152573.4; NP_689786.2.
DR UCSC; uc004amo.2; human. [Q8IZ41-1]
DR CTD; 158158; -.
DR DisGeNET; 158158; -.
DR GeneCards; RASEF; -.
DR HGNC; HGNC:26464; RASEF.
DR HPA; ENSG00000165105; Tissue enhanced (stomach).
DR MIM; 611344; gene.
DR neXtProt; NX_Q8IZ41; -.
DR OpenTargets; ENSG00000165105; -.
DR PharmGKB; PA134867201; -.
DR VEuPathDB; HostDB:ENSG00000165105; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000159488; -.
DR HOGENOM; CLU_023178_1_0_1; -.
DR InParanoid; Q8IZ41; -.
DR OMA; PKFTGHS; -.
DR OrthoDB; 1184845at2759; -.
DR PhylomeDB; Q8IZ41; -.
DR TreeFam; TF313106; -.
DR PathwayCommons; Q8IZ41; -.
DR SignaLink; Q8IZ41; -.
DR BioGRID-ORCS; 158158; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; RASEF; human.
DR EvolutionaryTrace; Q8IZ41; -.
DR GenomeRNAi; 158158; -.
DR Pharos; Q8IZ41; Tbio.
DR PRO; PR:Q8IZ41; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IZ41; protein.
DR Bgee; ENSG00000165105; Expressed in epithelial cell of pancreas and 130 other tissues.
DR Genevisible; Q8IZ41; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019003; F:GDP binding; IMP:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Cytoplasm;
KW GTP-binding; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..740
FT /note="Ras and EF-hand domain-containing protein"
FT /id="PRO_0000299577"
FT DOMAIN 8..42
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 42..77
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 82..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..356
FT /evidence="ECO:0000255"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:2PMY"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:2PMY"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0007744|PDB:2PMY"
FT BINDING 551..556
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2P5S"
FT BINDING 654..657
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2P5S"
FT BINDING 691..692
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:2P5S"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RI75"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RI75"
FT VAR_SEQ 145..189
FT /note="EEQVSTLYQNINLVEPRLIQPYEHVIKNFIREIRLQSTEMENLAI -> FGY
FT TISKPAFVFVRHLITLCALSWAKKEGRETLWTIEEGGAKMAE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027766"
FT VAR_SEQ 190..740
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027767"
FT VARIANT 262
FT /note="R -> C (in dbSNP:rs4146960)"
FT /evidence="ECO:0000269|PubMed:16015647"
FT /id="VAR_034858"
FT MUTAGEN 555
FT /note="S->N: Impairs nucleotide binding and perinuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:17448446"
FT MUTAGEN 600
FT /note="Q->L: Favors GTP association."
FT /evidence="ECO:0000269|PubMed:17448446"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:2PMY"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2PMY"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:2PMY"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2PMY"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2PMY"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2PMY"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:2PMY"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:2P5S"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:2P5S"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 604..613
FT /evidence="ECO:0007829|PDB:2P5S"
FT STRAND 615..622
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 626..630
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 632..642
FT /evidence="ECO:0007829|PDB:2P5S"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 659..664
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 672..682
FT /evidence="ECO:0007829|PDB:2P5S"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:2P5S"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:2P5S"
FT HELIX 697..708
FT /evidence="ECO:0007829|PDB:2P5S"
SQ SEQUENCE 740 AA; 82879 MW; 89AFCF4C159760F0 CRC64;
MEADGDGEEL ARLRSVFAAC DANRSGRLER EEFRALCTEL RVRPADAEAV FQRLDADRDG
AITFQEFARG FLGSLRGGRR RDWGPLDPAP AVSEAGPETH DSEEDEGDED AAAALATSCG
PASPGRAWQD FQARLGDEAK FIPREEQVST LYQNINLVEP RLIQPYEHVI KNFIREIRLQ
STEMENLAIA VKRAQDKAAM QLSELEEEMD QRIQAAEHKT RKDEKRKAEE ALSDLRRQYE
TEVGDLQVTI KKLRKLEEQS KRVSQKEDVA ALKKQIYDLS MENQKVKKDL LEAQTNIAFL
QSELDALKSD YADQSLNTER DLEIIRAYTE DRNSLERQIE ILQTANRKLH DSNDGLRSAL
ENSYSKFNRS LHINNISPGN TISRSSPKFI GHSPQPLGYD RSSRSSYVDE DCDSLALCDP
LQRTNCEVDS LPESCFDSGL STLRDPNEYD SEVEYKHQRG FQRSHGVQES FGGDASDTDV
PDIRDEETFG LEDVASVLDW KPQGSVSEGS IVSSSRKPIS ALSPQTDLVD DNAKSFSSQK
AYKIVLAGDA AVGKSSFLMR LCKNEFRENI SATLGVDFQM KTLIVDGERT VLQLWDTAGQ
ERFRSIAKSY FRKADGVLLL YDVTCEKSFL NIREWVDMIE DAAHETVPIM LVGNKADIRD
TAATEGQKCV PGHFGEKLAM TYGALFCETS AKDGSNIVEA VLHLAREVKK RTDKDDSRSI
TNLTGTNSKK SPQMKNCCNG
