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Reviewed, UniProtKB/Swiss-Prot O76054 (S14L2_HUMAN)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403SEC14-like protein 2
PRO_0000210755

Regions

Domain76 – 249174CRAL-TRIO
Domain275 – 383109GOLD

Natural variations

Natural variant111R → K: dbSNP rs757660.
VAR_024626

Experimental info

Sequence conflict361Y → H Ref.2

Secondary structure

....................................................................... 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O76054-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D846747EC8D1513E

FASTA40346,145
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

AL096881 mRNA. Translation: CAB51405.1.
AB033012 mRNA. Translation: BAA86500.2. Different initiation.
CR456571 mRNA. Translation: CAG30457.1.
AC004832 Genomic DNA. Translation: AAF19256.1.
PIRJC7708.
RefSeqNP_036561.1.
UniGeneHs.335614

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1O6UX-ray2.05A/C/E1-403[»]
1OLMX-ray1.95A/C/E1-403[»]
ModBaseSearch...

PTM databases

PhosphoSiteO76054.

Proteomic databases

PeptideAtlasO76054.

Genome annotation databases

EnsemblENSG00000100003. Homo sapiens. [Contig view]
GeneID23541.
KEGGhsa:23541.

Organism-specific databases

H-InvDBHIX0016371.
HGNCHGNC:10699. SEC14L2.
MIM607558. gene.
PharmGKBPA35622.
HUGESearch...
Search...
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases