S14L2_HUMAN
ID S14L2_HUMAN Reviewed; 403 AA.
AC O76054; B7Z8Q1; F5H3U4; Q53EQ2; Q6PD61; Q9ULN4;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=SEC14-like protein 2;
DE AltName: Full=Alpha-tocopherol-associated protein;
DE Short=TAP;
DE Short=hTAP;
DE AltName: Full=Squalene transfer protein;
DE AltName: Full=Supernatant protein factor;
DE Short=SPF;
GN Name=SEC14L2; Synonyms=C22orf6, KIAA1186, KIAA1658;
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), TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
RX PubMed=10829015; DOI=10.1074/jbc.m000851200;
RA Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A.;
RT "A novel human tocopherol-associated protein: cloning, in vitro expression,
RT and characterization.";
RL J. Biol. Chem. 275:25672-25680(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=11444841; DOI=10.1006/bbrc.2001.5162;
RA Yamauchi J., Iwamoto T., Kida S., Masushige S., Yamada K., Esashi T.;
RT "Tocopherol-associated protein is a ligand-dependent transcriptional
RT activator.";
RL Biochem. Biophys. Res. Commun. 285:295-299(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=11226224; DOI=10.1073/pnas.041620398;
RA Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., Inoue K.,
RA Arai H.;
RT "Supernatant protein factor, which stimulates the conversion of squalene to
RT lanosterol, is a cytosolic squalene transfer protein and enhances
RT cholesterol biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2244-2249(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LYS-11.
RC TISSUE=Liver;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-11.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=12429094; DOI=10.1016/s0969-2126(02)00884-5;
RA Stocker A., Tomizaki T., Schulze-Briese C., Baumann U.;
RT "Crystal structure of the human supernatant protein factor.";
RL Structure 10:1533-1540(2002).
CC -!- FUNCTION: Carrier protein. Binds to some hydrophobic molecules and
CC promotes their transfer between the different cellular sites. Binds
CC with high affinity to alpha-tocopherol. Also binds with a weaker
CC affinity to other tocopherols and to tocotrienols. May have a
CC transcriptional activatory activity via its association with alpha-
CC tocopherol. Probably recognizes and binds some squalene structure,
CC suggesting that it may regulate cholesterol biosynthesis by increasing
CC the transfer of squalene to a metabolic active pool in the cell.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in absence
CC of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O76054-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O76054-4; Sequence=VSP_042021;
CC Name=3;
CC IsoId=O76054-5; Sequence=VSP_045880;
CC -!- TISSUE SPECIFICITY: Widely expressed. Strong expression in liver, brain
CC and prostate. {ECO:0000269|PubMed:10829015}.
CC -!- DEVELOPMENTAL STAGE: Low expression in fetal tissues.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86500.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL096881; CAB51405.1; -; mRNA.
DR EMBL; AB033012; BAA86500.2; ALT_INIT; mRNA.
DR EMBL; CR456571; CAG30457.1; -; mRNA.
DR EMBL; AK303751; BAH14037.1; -; mRNA.
DR EMBL; AK223587; BAD97307.1; -; mRNA.
DR EMBL; AC004832; AAF19256.1; -; Genomic_DNA.
DR EMBL; BC058915; AAH58915.1; -; mRNA.
DR CCDS; CCDS13876.1; -. [O76054-1]
DR CCDS; CCDS46685.1; -. [O76054-4]
DR CCDS; CCDS56228.1; -. [O76054-5]
DR PIR; JC7708; JC7708.
DR RefSeq; NP_001191133.1; NM_001204204.2. [O76054-5]
DR RefSeq; NP_036561.1; NM_012429.4. [O76054-1]
DR RefSeq; NP_203740.1; NM_033382.2. [O76054-4]
DR PDB; 1O6U; X-ray; 2.05 A; A/C/E=1-403.
DR PDB; 1OLM; X-ray; 1.95 A; A/C/E=1-403.
DR PDB; 4OMJ; X-ray; 1.60 A; A/B=1-275.
DR PDB; 4OMK; X-ray; 1.75 A; A/B=1-275.
DR PDBsum; 1O6U; -.
DR PDBsum; 1OLM; -.
DR PDBsum; 4OMJ; -.
DR PDBsum; 4OMK; -.
DR AlphaFoldDB; O76054; -.
DR SMR; O76054; -.
DR BioGRID; 117085; 6.
DR IntAct; O76054; 2.
DR MINT; O76054; -.
DR STRING; 9606.ENSP00000478755; -.
DR DrugBank; DB14003; alpha-Tocopherol acetate.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB11635; Tocofersolan.
DR DrugBank; DB11251; Tocopherol.
DR DrugBank; DB00163; Vitamin E.
DR iPTMnet; O76054; -.
DR MetOSite; O76054; -.
DR PhosphoSitePlus; O76054; -.
DR SwissPalm; O76054; -.
DR BioMuta; SEC14L2; -.
DR EPD; O76054; -.
DR jPOST; O76054; -.
DR MassIVE; O76054; -.
DR MaxQB; O76054; -.
DR PaxDb; O76054; -.
DR PeptideAtlas; O76054; -.
DR PRIDE; O76054; -.
DR ProteomicsDB; 26377; -.
DR ProteomicsDB; 50365; -. [O76054-1]
DR ProteomicsDB; 50366; -. [O76054-4]
DR Antibodypedia; 10725; 275 antibodies from 24 providers.
DR DNASU; 23541; -.
DR Ensembl; ENST00000402592.7; ENSP00000383882.3; ENSG00000100003.18. [O76054-5]
DR Ensembl; ENST00000405717.7; ENSP00000385186.3; ENSG00000100003.18. [O76054-4]
DR Ensembl; ENST00000615189.5; ENSP00000478755.1; ENSG00000100003.18. [O76054-1]
DR GeneID; 23541; -.
DR KEGG; hsa:23541; -.
DR MANE-Select; ENST00000615189.5; ENSP00000478755.1; NM_012429.5; NP_036561.1.
DR UCSC; uc003ahq.5; human. [O76054-1]
DR CTD; 23541; -.
DR DisGeNET; 23541; -.
DR GeneCards; SEC14L2; -.
DR HGNC; HGNC:10699; SEC14L2.
DR HPA; ENSG00000100003; Tissue enhanced (epididymis, liver).
DR MIM; 607558; gene.
DR neXtProt; NX_O76054; -.
DR OpenTargets; ENSG00000100003; -.
DR PharmGKB; PA35622; -.
DR VEuPathDB; HostDB:ENSG00000100003; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000160650; -.
DR HOGENOM; CLU_014001_2_1_1; -.
DR InParanoid; O76054; -.
DR OMA; CECAGGC; -.
DR PhylomeDB; O76054; -.
DR TreeFam; TF313988; -.
DR PathwayCommons; O76054; -.
DR SignaLink; O76054; -.
DR BioGRID-ORCS; 23541; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; SEC14L2; human.
DR EvolutionaryTrace; O76054; -.
DR GeneWiki; SEC14L2; -.
DR GenomeRNAi; 23541; -.
DR Pharos; O76054; Tbio.
DR PRO; PR:O76054; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O76054; protein.
DR Bgee; ENSG00000100003; Expressed in right lobe of liver and 131 other tissues.
DR ExpressionAtlas; O76054; baseline and differential.
DR Genevisible; O76054; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; NAS:UniProtKB.
DR GO; GO:0008431; F:vitamin E binding; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; NAS:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Lipid-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1..403
FT /note="SEC14-like protein 2"
FT /id="PRO_0000210755"
FT DOMAIN 76..249
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 275..383
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT MOD_RES 51
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 257
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 393
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT VAR_SEQ 58..140
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045880"
FT VAR_SEQ 361..403
FT /note="YVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK -> CKYLC
FT LGNALKPHVQLSACEVPLPPWIFGSEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042021"
FT VARIANT 11
FT /note="R -> K (in dbSNP:rs757660)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.8"
FT /id="VAR_024626"
FT CONFLICT 36
FT /note="Y -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:4OMJ"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:4OMJ"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 117..142
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1OLM"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4OMJ"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:4OMJ"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1OLM"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:1OLM"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:1OLM"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:1OLM"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:1OLM"
SQ SEQUENCE 403 AA; 46145 MW; D846747EC8D1513E CRC64;
MSGRVGDLSP RQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV
EFRKQKDIDN IISWQPPEVI QQYLSGGMCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL
LRTKMRECEL LLQECAHQTT KLGRKVETIT IIYDCEGLGL KHLWKPAVEA YGEFLCMFEE
NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQVPVE
YGGTMTDPDG NPKCKSKINY GGDIPRKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG
CVLRWQFMSD GADVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHLVPED GTLTCSDPGI
YVLRFDNTYS FIHAKKVNFT VEVLLPDKAS EEKMKQLGAG TPK
