S14L2_MOUSE
ID S14L2_MOUSE Reviewed; 403 AA.
AC Q99J08;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=SEC14-like protein 2;
DE AltName: Full=Alpha-tocopherol-associated protein;
DE Short=TAP;
GN Name=Sec14l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-51; LYS-253; LYS-257
RP AND LYS-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Cytoplasmic in absence of alpha-tocopherol, and nuclear in
CC presence of alpha-tocopherol. {ECO:0000250}.
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DR EMBL; BC005759; AAH05759.1; -; mRNA.
DR CCDS; CCDS24377.1; -.
DR RefSeq; NP_653103.1; NM_144520.2.
DR AlphaFoldDB; Q99J08; -.
DR SMR; Q99J08; -.
DR BioGRID; 212457; 3.
DR STRING; 10090.ENSMUSP00000003681; -.
DR iPTMnet; Q99J08; -.
DR PhosphoSitePlus; Q99J08; -.
DR SwissPalm; Q99J08; -.
DR EPD; Q99J08; -.
DR jPOST; Q99J08; -.
DR MaxQB; Q99J08; -.
DR PaxDb; Q99J08; -.
DR PeptideAtlas; Q99J08; -.
DR PRIDE; Q99J08; -.
DR ProteomicsDB; 253349; -.
DR DNASU; 67815; -.
DR Ensembl; ENSMUST00000003681; ENSMUSP00000003681; ENSMUSG00000003585.
DR GeneID; 67815; -.
DR KEGG; mmu:67815; -.
DR UCSC; uc007huh.1; mouse.
DR CTD; 23541; -.
DR MGI; MGI:1915065; Sec14l2.
DR VEuPathDB; HostDB:ENSMUSG00000003585; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000160650; -.
DR HOGENOM; CLU_014001_2_1_1; -.
DR InParanoid; Q99J08; -.
DR OMA; CECAGGC; -.
DR OrthoDB; 1133487at2759; -.
DR PhylomeDB; Q99J08; -.
DR TreeFam; TF313988; -.
DR BioGRID-ORCS; 67815; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Sec14l2; mouse.
DR PRO; PR:Q99J08; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99J08; protein.
DR Bgee; ENSMUSG00000003585; Expressed in skin of snout and 202 other tissues.
DR Genevisible; Q99J08; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; ISO:MGI.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:MGI.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 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 Pfam; PF00650; CRAL_TRIO; 1.
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 1: Evidence at protein level;
KW Activator; Cytoplasm; Lipid-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..403
FT /note="SEC14-like protein 2"
FT /id="PRO_0000210756"
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 11
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 51
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 257
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 393
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 403 AA; 46300 MW; 42E0BBAFE3004841 CRC64;
MSGRVGDLSP KQEEALAKFR ENVQDVLPTL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV
EFRKQKDIDK IISWQPPEVI QQYLSGGRCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL
LRTKMRDCEL LLQECIQQTT KLGKKIETIT MIYDCEGLGL KHLWKPAVEA YGEFLTMFEE
NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRRKIMVL GANWKEVLLK HISPDQLPVE
YGGTMTDPDG NPKCKSKINY GGDIPKQYYV RDQVKQQYEH TVQVSRGSSH QVEYEILFPG
CVLRWQFMSE GSDVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHMVPED GTLTCSEPGI
YVLRFDNTYS FIHAKKVSFT VEVLLPDKAA EEKMNQQGAD TPK
