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   27-MAR-2024, entry version 198.
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; 24.
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   GlyGen; O76054; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000478755; -.
DR   PeptideAtlas; O76054; -.
DR   ProteomicsDB; 26377; -.
DR   ProteomicsDB; 50365; -. [O76054-1]
DR   ProteomicsDB; 50366; -. [O76054-4]
DR   Pumba; O76054; -.
DR   Antibodypedia; 10725; 307 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   AGR; HGNC:10699; -.
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; NMPKREL; -.
DR   OrthoDB; 6048at2759; -.
DR   PhylomeDB; O76054; -.
DR   TreeFam; TF313988; -.
DR   PathwayCommons; O76054; -.
DR   SignaLink; O76054; -.
DR   SIGNOR; O76054; -.
DR   BioGRID-ORCS; 23541; 18 hits in 1156 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 133 other cell types or tissues.
DR   ExpressionAtlas; O76054; baseline and differential.
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 DNA-templated transcription; 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; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 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   PANTHER; PTHR23324; SEC14 RELATED PROTEIN; 1.
DR   PANTHER; PTHR23324:SF90; SEC14-LIKE PROTEIN 2; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   Genevisible; O76054; HS.
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
//