S14L2_BOVIN
ID S14L2_BOVIN Reviewed; 403 AA.
AC P58875; Q32KW6; Q867A0;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=SEC14-like protein 2;
DE AltName: Full=Alpha-tocopherol-associated protein;
DE Short=TAP;
DE Short=bTAP;
GN Name=SEC14L2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 178-195 AND 335-353.
RC TISSUE=Liver;
RX PubMed=10829015; DOI=10.1074/jbc.m000851200;
RA Zimmer S., Stocker A., Sarbolouki M.N., Spycher S.E., Sassoon J., Azzi A.;
RT "A novel human tocopherol-associated protein: cloning, in vitro expression,
RT and characterization.";
RL J. Biol. Chem. 275:25672-25680(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-387.
RC TISSUE=Liver;
RA Meadus J., MacInnis R., Dubeski P., Hidiroglou N., Madere R.;
RT "Induction of hepatic tocopherol associated protein (TAP) mRNA but not
RT alpha-tocopherol transfer protein (TTP) mRNA in cattle fed increasing
RT levels of vitamin E.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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.
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}.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; AF432353; AAO31942.1; -; mRNA.
DR EMBL; BC109891; AAI09892.1; -; mRNA.
DR EMBL; AF487977; AAL90886.1; -; mRNA.
DR RefSeq; NP_808812.2; NM_177943.2.
DR RefSeq; XP_010812385.1; XM_010814083.2.
DR RefSeq; XP_015331029.1; XM_015475543.1.
DR AlphaFoldDB; P58875; -.
DR SMR; P58875; -.
DR STRING; 9913.ENSBTAP00000051657; -.
DR PaxDb; P58875; -.
DR PeptideAtlas; P58875; -.
DR GeneID; 282469; -.
DR KEGG; bta:282469; -.
DR CTD; 23541; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_2_1_1; -.
DR InParanoid; P58875; -.
DR OrthoDB; 1133487at2759; -.
DR TreeFam; TF313988; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; Direct protein sequencing; Lipid-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transport.
FT CHAIN 1..403
FT /note="SEC14-like protein 2"
FT /id="PRO_0000210754"
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:0000250|UniProtKB:Q99J08"
FT MOD_RES 51
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 257
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT MOD_RES 393
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J08"
FT CONFLICT 193
FT /note="K -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="N -> S (in Ref. 3; AAL90886)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> D (in Ref. 3; AAL90886)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="L -> S (in Ref. 2; AAI09892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46200 MW; 67C28EFC173E1CD9 CRC64;
MSGRVGDLSP KQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARNFNLQ KSEAMLRKHV
EFRKQKDIDN IMSWQPPEVV QQYLSGGMCG YDLEGSPIWY DIIGPLDAKG LLLSASKQDL
FKTKMRDCEL LLQECVRQTE KMGKKIEATT LIYDCEGLGL KHLWKPAVEA YGEFLCMFEE
NYPETLKRLF IVKAPKLFPV AYNLVKPFLS EDTRKKIQVL GANWKEVLLK YISPDQLPVE
YGGTMTDPDG NPKCKSKINY GGDIPKKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG
CVLRWQFMSD GSDIGFGIFL KTKVGERQRA GEMREVLPSQ RYNAHLVPED GSLTCSDPGI
YVLRFDNTYS FIHAKKVSFT VEVLLPDKAL EEKMQQLGAV TPK
