Reviewed, UniProtKB/Swiss-Prot O76054 (S14L2_HUMAN)

Names and origin

Protein names

Recommended name:
    SEC14-like protein 2
Alternative name(s):
    Alpha-tocopherol-associated protein
      Short name=TAP
      Short name=hTAP
    Supernatant protein factor
      Short name=SPF
    Squalene transfer protein

Gene names

Name:	SEC14L2
Synonyms:	C22orf6, KIAA1186, KIAA1658

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm. Nucleus. Note= Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.
Tissue specificity	Widely expressed. Strong expression in liver, brain and prostate.
Developmental stage	Low expression in fetal tissues.
Sequence similarities	Contains 1 CRAL-TRIO domain. Contains 1 GOLD domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding
Molecular function	Activator
Technical term	3D-structure
Gene Ontology (GO)
Biological process	positive regulation of transcription, DNA-dependent Ref.2 Non-traceable author statement. Source: UniProtKB regulation of cholesterol biosynthetic process Ref.3 Non-traceable author statement. Source: UniProtKB transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.1 Non-traceable author statement. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: InterPro nucleus Ref.2 Non-traceable author statement. Source: UniProtKB
Molecular function	phospholipid binding Non-traceable author statement. Source: UniProtKB transcription activator activity Ref.2 Non-traceable author statement. Source: UniProtKB transporter activity Inferred from electronic annotation. Source: InterPro vitamin E binding Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 403

403

SEC14-like protein 2

PRO_0000210755

Regions

Domain

76 – 249

174

CRAL-TRIO

Domain

275 – 383

109

GOLD

Natural variations

Natural variant

11

1

R → K: dbSNP rs757660.

VAR_024626

Experimental info

Sequence conflict

36

1

Y → H Ref.2

Secondary structure

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403

Helix Strand Turn

Details...

Helix

10 – 22

13

Helix

24 – 29

6

Helix

35 – 44

10

Turn

45 – 47

3

Helix

49 – 66

18

Helix

68 – 73

6

Helix

78 – 83

6

Beta strand

86 – 91

6

Beta strand

97 – 102

6

Helix

108 – 114

7

Helix

117 – 142

26

Beta strand

149 – 154

6

Helix

160 – 163

4

Helix

165 – 181

17

Beta strand

186 – 193

8

Helix

198 – 205

8

Helix

206 – 208

3

Helix

211 – 215

5

Beta strand

217 – 219

3

Helix

224 – 228

5

Turn

229 – 231

3

Helix

234 – 236

3

Helix

239 – 241

3

Beta strand

243 – 245

3

Turn

255 – 257

3

Helix

266 – 268

3

Beta strand

279 – 284

6

Beta strand

289 – 296

8

Beta strand

301 – 312

12

Beta strand

314 – 320

7

Helix

330 – 332

3

Beta strand

333 – 342

10

Turn

344 – 346

3

Beta strand

349 – 355

7

Beta strand

359 – 366

8

Beta strand

374 – 384

11

Helix

388 – 396

9

Sequences

	Sequence		Length	Mass (Da)
	O76054-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D846747EC8D1513E	FASTA	403	46,145
	10 20 30 40 50 60 MSGRVGDLSP RQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV 70 80 90 100 110 120 EFRKQKDIDN IISWQPPEVI QQYLSGGMCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL 130 140 150 160 170 180 LRTKMRECEL LLQECAHQTT KLGRKVETIT IIYDCEGLGL KHLWKPAVEA YGEFLCMFEE 190 200 210 220 230 240 NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQVPVE 250 260 270 280 290 300 YGGTMTDPDG NPKCKSKINY GGDIPRKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG 310 320 330 340 350 360 CVLRWQFMSD GADVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHLVPED GTLTCSDPGI 370 380 390 400 YVLRFDNTYS FIHAKKVNFT VEVLLPDKAS EEKMKQLGAG TPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization." Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A. J. Biol. Chem. 275:25672-25680(2000) [PubMed: 10829015] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION.
[2]	"Tocopherol-associated protein is a ligand-dependent transcriptional activator." Yamauchi J., Iwamoto T., Kida S., Masushige S., Yamada K., Esashi T. Biochem. Biophys. Res. Commun. 285:295-299(2001) [PubMed: 11444841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Liver.
[3]	"Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis." Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., Inoue K., Arai H. Proc. Natl. Acad. Sci. U.S.A. 98:2244-2249(2001) [PubMed: 11226224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Liver.
[4]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed: 10574461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	Ohara O., Nagase T., Kikuno R. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"Crystal structure of the human supernatant protein factor." Stocker A., Tomizaki T., Schulze-Briese C., Baumann U. Structure 10:1533-1540(2002) [PubMed: 12429094] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL096881 mRNA. Translation: CAB51405.1.
AB033012 mRNA. Translation: BAA86500.2. Different initiation.
CR456571 mRNA. Translation: CAG30457.1.
AC004832 Genomic DNA. Translation: AAF19256.1.

PIR

JC7708.

RefSeq

NP_036561.1.

UniGene

Hs.335614

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O6U	X-ray	2.05	A/C/E	1-403	[»]
1OLM	X-ray	1.95	A/C/E	1-403	[»]

ModBase

Search...

PTM databases

PhosphoSite

O76054.

Proteomic databases

PeptideAtlas

O76054.

Genome annotation databases

Ensembl

ENSG00000100003. Homo sapiens. [Contig view]

GeneID

23541.

KEGG

hsa:23541.

Organism-specific databases

H-InvDB

HIX0016371.

HGNC

HGNC:10699. SEC14L2.

MIM

607558. gene.

PharmGKB

PA35622.

HUGE

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GenAtlas

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GeneCards

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Phylogenomic databases