O76054 (S14L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SEC14-like protein 2

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

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.
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. Ref.1
Developmental stage	Low expression in fetal tissues.
Sequence similarities	Contains 1 CRAL-TRIO domain. Contains 1 GOLD domain.
Sequence caution	The sequence BAA86500.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O76054-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O76054-4)

The sequence of this isoform differs from the canonical sequence as follows:
     361-403: YVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK → CKYLCLGNALKPHVQLSACEVPLPPWIFGSEC

Note: No experimental confirmation available.

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

Alternative sequence

361 – 403

43

YVLRF…AGTPK → CKYLCLGNALKPHVQLSACE VPLPPWIFGSEC in isoform 2.

VSP_042021

Natural variant

11

1

R → K. Ref.7
Corresponds to variant rs757660 [ dbSNP | Ensembl ].

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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 11A833345968FE5A	FASTA	392	44,748
	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 CKYLCLGNAL KPHVQLSACE VPLPPWIFGS EC

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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1). 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:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-11. Tissue: Kidney.
[8]	"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].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[10]	"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

EMBL
GenBank
DDBJ

AL096881 mRNA. Translation: CAB51405.1.
AB033012 mRNA. Translation: BAA86500.2. Different initiation.
CR456571 mRNA. Translation: CAG30457.1.
AK223587 mRNA. Translation: BAD97307.1.
AC004832 Genomic DNA. Translation: AAF19256.1.
BC058915 mRNA. Translation: AAH58915.1.

IPI

IPI00018314.

PIR

JC7708.

RefSeq

NP_001191133.1. NM_001204204.1.
NP_036561.1. NM_012429.3.
NP_203740.1. NM_033382.2.

UniGene

Hs.335614.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O76054.

SMR

O76054. Positions 1-397.

ModBase

Search...

Protein-protein interaction databases

STRING

O76054.

PTM databases

PhosphoSite

O76054.

Proteomic databases

PeptideAtlas

O76054.

PRIDE

O76054.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312932; ENSP00000316203; ENSG00000100003.

GeneID

23541.

KEGG

hsa:23541.

UCSC

uc003ahr.1. human.

Organism-specific databases

CTD

23541.

GeneCards

GC22P030792.

H-InvDB

HIX0016371.

HGNC

HGNC:10699. SEC14L2.

MIM

607558. gene.

neXtProt

NX_O76054.

PharmGKB

PA35622.

HUGE

Search...
Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04503.

GeneTree

ENSGT00550000074580.

HOGENOM

HBG506277.

HOVERGEN

HBG055336.

InParanoid

O76054.

OMA

NFTVEVL.

OrthoDB

EOG4QC15C.

PhylomeDB

O76054.

Gene expression databases

ArrayExpress

O76054.

Bgee

O76054.

CleanEx

HS_SEC14L2.

Genevestigator

O76054.

GermOnline

ENSG00000100003. Homo sapiens.

Family and domain databases

InterPro

IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR009038. GOLD.
[Graphical view]

Gene3D

G3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
G3DSA:1.10.8.20. G3DSA:1.10.8.20. 1 hit.

Pfam

PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]

PRINTS

PR00180. CRETINALDHBP.

SMART

SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]

SUPFAM

SSF52087. CRAL_TRIO_C. 1 hit.
SSF101576. GOLD. 1 hit.
SSF46938. Sec14p_like_N. 1 hit.

PROSITE

PS50191. CRAL_TRIO. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00163. Vitamin E.

NextBio

46048.

SOURCE

Search...

Entry information

Entry name

S14L2_HUMAN

Accession

Primary (citable) accession number: O76054
Secondary accession number(s): Q53EQ2, Q6PD61, Q9ULN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.