Full text data of SEC14L4
SEC14L4
(TAP3)
[Confidence: low (only semi-automatic identification from reviews)]
SEC14-like protein 4 (Tocopherol-associated protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
SEC14-like protein 4 (Tocopherol-associated protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UDX3
ID S14L4_HUMAN Reviewed; 406 AA.
AC Q9UDX3; A5D6W7; A6NCV4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=SEC14-like protein 4;
DE AltName: Full=Tocopherol-associated protein 3;
GN Name=SEC14L4; Synonyms=TAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12757856; DOI=10.1016/S0891-5849(03)00173-4;
RA Kempna P., Zingg J.-M., Ricciarelli R., Hierl M., Saxena S., Azzi A.;
RT "Cloning of novel human SEC14p-like proteins: ligand binding and
RT functional properties.";
RL Free Radic. Biol. Med. 34:1458-1472(2003).
RN [2]
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable hydrophobic ligand-binding protein; may play a
CC role in the transport of hydrophobic ligands like tocopherol,
CC squalene and phospholipids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UDX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UDX3-2; Sequence=VSP_045200;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY158085; AAO21869.1; -; mRNA.
DR EMBL; AC004832; AAF19259.1; -; Genomic_DNA.
DR EMBL; BC139912; AAI39913.1; -; mRNA.
DR RefSeq; NP_001154840.1; NM_001161368.1.
DR RefSeq; NP_777637.1; NM_174977.3.
DR UniGene; Hs.517541; -.
DR ProteinModelPortal; Q9UDX3; -.
DR SMR; Q9UDX3; 1-397.
DR STRING; 9606.ENSP00000255858; -.
DR DrugBank; DB00163; Vitamin E.
DR PhosphoSite; Q9UDX3; -.
DR DMDM; 29337003; -.
DR PaxDb; Q9UDX3; -.
DR PRIDE; Q9UDX3; -.
DR DNASU; 284904; -.
DR Ensembl; ENST00000255858; ENSP00000255858; ENSG00000133488.
DR Ensembl; ENST00000381982; ENSP00000371412; ENSG00000133488.
DR GeneID; 284904; -.
DR KEGG; hsa:284904; -.
DR UCSC; uc003aid.2; human.
DR CTD; 284904; -.
DR GeneCards; GC22M030884; -.
DR HGNC; HGNC:20627; SEC14L4.
DR MIM; 612825; gene.
DR neXtProt; NX_Q9UDX3; -.
DR PharmGKB; PA134979694; -.
DR eggNOG; NOG276405; -.
DR HOGENOM; HOG000232201; -.
DR HOVERGEN; HBG055336; -.
DR InParanoid; Q9UDX3; -.
DR OMA; LLHECEL; -.
DR OrthoDB; EOG7N8ZVD; -.
DR PhylomeDB; Q9UDX3; -.
DR GenomeRNAi; 284904; -.
DR NextBio; 95165; -.
DR PRO; PR:Q9UDX3; -.
DR ArrayExpress; Q9UDX3; -.
DR Bgee; Q9UDX3; -.
DR CleanEx; HS_SEC14L4; -.
DR Genevestigator; Q9UDX3; -.
DR GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001071; CRAL-bd_toc_tran.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR PRINTS; PR00180; CRETINALDHBP.
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 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Lipid-binding; Polymorphism;
KW Reference proteome; Transport.
FT CHAIN 1 406 SEC14-like protein 4.
FT /FTId=PRO_0000210760.
FT DOMAIN 76 249 CRAL-TRIO.
FT DOMAIN 252 383 GOLD.
FT VAR_SEQ 361 406 Missing (in isoform 2).
FT /FTId=VSP_045200.
FT VARIANT 3 3 S -> G (in dbSNP:rs9608956).
FT /FTId=VAR_024629.
FT VARIANT 124 124 R -> G (in dbSNP:rs9606739).
FT /FTId=VAR_051914.
FT VARIANT 200 200 V -> M (in dbSNP:rs17738540).
FT /FTId=VAR_051915.
FT VARIANT 211 211 E -> K (in dbSNP:rs17738527).
FT /FTId=VAR_051916.
SQ SEQUENCE 406 AA; 46644 MW; 7C8763DDA202EB5A CRC64;
MSSRVGDLSP QQQEALARFR ENLQDLLPIL PNADDYFLLR WLRARNFDLQ KSEDMLRRHM
EFRKQQDLDN IVTWQPPEVI QLYDSGGLCG YDYEGCPVYF NIIGSLDPKG LLLSASKQDM
IRKRIKVCEL LLHECELQTQ KLGRKIEMAL MVFDMEGLSL KHLWKPAVEV YQQFFSILEA
NYPETLKNLI VIRAPKLFPV AFNLVKSFMS EETRRKIVIL GDNWKQELTK FISPDQLPVE
FGGTMTDPDG NPKCLTKINY GGEVPKSYYL CEQVRLQYEH TRSVGRGSSL QVENEILFPG
CVLRWQFASD GGDIGFGVFL KTKMGEQQSA REMTEVLPSQ RYNAHMVPED GSLTCLQAGV
YVLRFDNTYS RMHAKKLSYT VEVLLPDKAS EETLQSLKAM RPSPTQ
//
ID S14L4_HUMAN Reviewed; 406 AA.
AC Q9UDX3; A5D6W7; A6NCV4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=SEC14-like protein 4;
DE AltName: Full=Tocopherol-associated protein 3;
GN Name=SEC14L4; Synonyms=TAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12757856; DOI=10.1016/S0891-5849(03)00173-4;
RA Kempna P., Zingg J.-M., Ricciarelli R., Hierl M., Saxena S., Azzi A.;
RT "Cloning of novel human SEC14p-like proteins: ligand binding and
RT functional properties.";
RL Free Radic. Biol. Med. 34:1458-1472(2003).
RN [2]
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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable hydrophobic ligand-binding protein; may play a
CC role in the transport of hydrophobic ligands like tocopherol,
CC squalene and phospholipids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UDX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UDX3-2; Sequence=VSP_045200;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY158085; AAO21869.1; -; mRNA.
DR EMBL; AC004832; AAF19259.1; -; Genomic_DNA.
DR EMBL; BC139912; AAI39913.1; -; mRNA.
DR RefSeq; NP_001154840.1; NM_001161368.1.
DR RefSeq; NP_777637.1; NM_174977.3.
DR UniGene; Hs.517541; -.
DR ProteinModelPortal; Q9UDX3; -.
DR SMR; Q9UDX3; 1-397.
DR STRING; 9606.ENSP00000255858; -.
DR DrugBank; DB00163; Vitamin E.
DR PhosphoSite; Q9UDX3; -.
DR DMDM; 29337003; -.
DR PaxDb; Q9UDX3; -.
DR PRIDE; Q9UDX3; -.
DR DNASU; 284904; -.
DR Ensembl; ENST00000255858; ENSP00000255858; ENSG00000133488.
DR Ensembl; ENST00000381982; ENSP00000371412; ENSG00000133488.
DR GeneID; 284904; -.
DR KEGG; hsa:284904; -.
DR UCSC; uc003aid.2; human.
DR CTD; 284904; -.
DR GeneCards; GC22M030884; -.
DR HGNC; HGNC:20627; SEC14L4.
DR MIM; 612825; gene.
DR neXtProt; NX_Q9UDX3; -.
DR PharmGKB; PA134979694; -.
DR eggNOG; NOG276405; -.
DR HOGENOM; HOG000232201; -.
DR HOVERGEN; HBG055336; -.
DR InParanoid; Q9UDX3; -.
DR OMA; LLHECEL; -.
DR OrthoDB; EOG7N8ZVD; -.
DR PhylomeDB; Q9UDX3; -.
DR GenomeRNAi; 284904; -.
DR NextBio; 95165; -.
DR PRO; PR:Q9UDX3; -.
DR ArrayExpress; Q9UDX3; -.
DR Bgee; Q9UDX3; -.
DR CleanEx; HS_SEC14L4; -.
DR Genevestigator; Q9UDX3; -.
DR GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001071; CRAL-bd_toc_tran.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR PRINTS; PR00180; CRETINALDHBP.
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 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Lipid-binding; Polymorphism;
KW Reference proteome; Transport.
FT CHAIN 1 406 SEC14-like protein 4.
FT /FTId=PRO_0000210760.
FT DOMAIN 76 249 CRAL-TRIO.
FT DOMAIN 252 383 GOLD.
FT VAR_SEQ 361 406 Missing (in isoform 2).
FT /FTId=VSP_045200.
FT VARIANT 3 3 S -> G (in dbSNP:rs9608956).
FT /FTId=VAR_024629.
FT VARIANT 124 124 R -> G (in dbSNP:rs9606739).
FT /FTId=VAR_051914.
FT VARIANT 200 200 V -> M (in dbSNP:rs17738540).
FT /FTId=VAR_051915.
FT VARIANT 211 211 E -> K (in dbSNP:rs17738527).
FT /FTId=VAR_051916.
SQ SEQUENCE 406 AA; 46644 MW; 7C8763DDA202EB5A CRC64;
MSSRVGDLSP QQQEALARFR ENLQDLLPIL PNADDYFLLR WLRARNFDLQ KSEDMLRRHM
EFRKQQDLDN IVTWQPPEVI QLYDSGGLCG YDYEGCPVYF NIIGSLDPKG LLLSASKQDM
IRKRIKVCEL LLHECELQTQ KLGRKIEMAL MVFDMEGLSL KHLWKPAVEV YQQFFSILEA
NYPETLKNLI VIRAPKLFPV AFNLVKSFMS EETRRKIVIL GDNWKQELTK FISPDQLPVE
FGGTMTDPDG NPKCLTKINY GGEVPKSYYL CEQVRLQYEH TRSVGRGSSL QVENEILFPG
CVLRWQFASD GGDIGFGVFL KTKMGEQQSA REMTEVLPSQ RYNAHMVPED GSLTCLQAGV
YVLRFDNTYS RMHAKKLSYT VEVLLPDKAS EETLQSLKAM RPSPTQ
//
MIM
612825
*RECORD*
*FIELD* NO
612825
*FIELD* TI
*612825 SEC14-LIKE 4; SEC14L4
;;SEC14, S. CEREVISIAE, HOMOLOG OF, 4;;
TOCOPHEROL-ASSOCIATED PROTEIN 3; TAP3
read more*FIELD* TX
CLONING
By database analysis of the region surrounding human SEC14L2 (607558),
followed by RT-PCR analysis of human lung total RNA, Kempna et al.
(2003) cloned SEC14L3 (612824) and SEC14L4, which they called TAP2 and
TAP3, respectively. The 406-amino acid SEC14L4 protein has a conserved
CRAL/TRIO domain and shares 80% similarity with SEC14L2. All 3 proteins
share residues glu185 and lys216, which are predicted to play a role in
phospholipid binding and transfer activity in S. cerevisiae Sec14.
RT-PCR of human tissues and cell lines detected high SEC14L4 expression
in all tissues examined. Immunocytochemical studies localized SEC14L4 to
intracellular membranes of the cytoplasm in HeLa cells, including
partial localization to the ER and Golgi, with more intense staining
surrounding but not within the nucleus.
GENE FUNCTION
Kempna et al. (2003) showed that in HeLa cells deletion of the
C-terminal Golgi dynamics (GOLD) domain changed SEC14L4 localization
with decreased staining surrounding the nucleus and a more dispersed
staining throughout the cell. They suggested that the SEC14L4 GOLD
domain may play a role in docking to other proteins or in intracellular
transport of bound ligands. Using several assays, Kempna et al. (2003)
demonstrated that SEC14L3 bound tocopherol, squalene, and phospholipids
(phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol).
Although SEC14L4 bound phospholipids, it failed to complement an S.
cerevisiae temperature-sensitive Sec14 allele in yeast. Using
immunoprecipitation assays, Kempna et al. (2003) showed that SEC14L4 may
interact with and regulate phosphatidylinositol 3-kinase activity and
that SEC14L4 displayed low basal GTPase activity.
GENE STRUCTURE
Kempna et al. (2003) determined that the SEC14L4 gene contains 12 exons.
MAPPING
By database analysis, Kempna et al. (2003) mapped the SEC14L4 gene to
chromosome 22q12.1-qter, where it lies within 100 kb of the SEC14L2 and
SEC14L3 genes.
*FIELD* SA
Ye et al. (2004)
*FIELD* RF
1. Kempna, P.; Zingg, J.-M.; Ricciarelli, R.; Hierl, M.; Saxena, S.;
Azzi, A.: Cloning of novel human Sec14p-like proteins: ligand binding
and functional properties. Free Radical Biol. Med. 34: 1458-1472,
2003.
2. Ye, X.; Ji, C.; Yin, G.; Tang, R.; Zeng, L.; Gu, S.; Ying, K.;
Xie, Y.; Zhao, R. C.; Mao, Y.: Characterization of a human Sec14-like
protein cDNA SEC14L3 highly homologous to human SPF/TAP. Molec. Biol.
Reports 31: 59-63, 2004.
*FIELD* CD
Dorothy S. Reilly: 5/28/2009
*FIELD* ED
wwang: 05/28/2009
*RECORD*
*FIELD* NO
612825
*FIELD* TI
*612825 SEC14-LIKE 4; SEC14L4
;;SEC14, S. CEREVISIAE, HOMOLOG OF, 4;;
TOCOPHEROL-ASSOCIATED PROTEIN 3; TAP3
read more*FIELD* TX
CLONING
By database analysis of the region surrounding human SEC14L2 (607558),
followed by RT-PCR analysis of human lung total RNA, Kempna et al.
(2003) cloned SEC14L3 (612824) and SEC14L4, which they called TAP2 and
TAP3, respectively. The 406-amino acid SEC14L4 protein has a conserved
CRAL/TRIO domain and shares 80% similarity with SEC14L2. All 3 proteins
share residues glu185 and lys216, which are predicted to play a role in
phospholipid binding and transfer activity in S. cerevisiae Sec14.
RT-PCR of human tissues and cell lines detected high SEC14L4 expression
in all tissues examined. Immunocytochemical studies localized SEC14L4 to
intracellular membranes of the cytoplasm in HeLa cells, including
partial localization to the ER and Golgi, with more intense staining
surrounding but not within the nucleus.
GENE FUNCTION
Kempna et al. (2003) showed that in HeLa cells deletion of the
C-terminal Golgi dynamics (GOLD) domain changed SEC14L4 localization
with decreased staining surrounding the nucleus and a more dispersed
staining throughout the cell. They suggested that the SEC14L4 GOLD
domain may play a role in docking to other proteins or in intracellular
transport of bound ligands. Using several assays, Kempna et al. (2003)
demonstrated that SEC14L3 bound tocopherol, squalene, and phospholipids
(phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol).
Although SEC14L4 bound phospholipids, it failed to complement an S.
cerevisiae temperature-sensitive Sec14 allele in yeast. Using
immunoprecipitation assays, Kempna et al. (2003) showed that SEC14L4 may
interact with and regulate phosphatidylinositol 3-kinase activity and
that SEC14L4 displayed low basal GTPase activity.
GENE STRUCTURE
Kempna et al. (2003) determined that the SEC14L4 gene contains 12 exons.
MAPPING
By database analysis, Kempna et al. (2003) mapped the SEC14L4 gene to
chromosome 22q12.1-qter, where it lies within 100 kb of the SEC14L2 and
SEC14L3 genes.
*FIELD* SA
Ye et al. (2004)
*FIELD* RF
1. Kempna, P.; Zingg, J.-M.; Ricciarelli, R.; Hierl, M.; Saxena, S.;
Azzi, A.: Cloning of novel human Sec14p-like proteins: ligand binding
and functional properties. Free Radical Biol. Med. 34: 1458-1472,
2003.
2. Ye, X.; Ji, C.; Yin, G.; Tang, R.; Zeng, L.; Gu, S.; Ying, K.;
Xie, Y.; Zhao, R. C.; Mao, Y.: Characterization of a human Sec14-like
protein cDNA SEC14L3 highly homologous to human SPF/TAP. Molec. Biol.
Reports 31: 59-63, 2004.
*FIELD* CD
Dorothy S. Reilly: 5/28/2009
*FIELD* ED
wwang: 05/28/2009