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   27-MAR-2024, entry version 130.
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; 9913-ENSBTAP00000051657; -.
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   TreeFam; TF313988; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 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   PANTHER; PTHR23324; SEC14 RELATED PROTEIN; 1.
DR   PANTHER; PTHR23324:SF90; SEC14-LIKE PROTEIN 2; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 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
//