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P58875

- S14L2_BOVIN

UniProt

P58875 - S14L2_BOVIN

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Protein
SEC14-like protein 2
Gene
SEC14L2
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity.

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW
  2. transporter activity Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SEC14-like protein 2
Alternative name(s):
Alpha-tocopherol-associated protein
Short name:
TAP
Short name:
bTAP
Gene namesi
Name:SEC14L2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 17

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. integral component of membrane Source: InterPro
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403SEC14-like protein 2
PRO_0000210754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111N6-succinyllysine By similarity
Modified residuei51 – 511N6-succinyllysine By similarity
Modified residuei253 – 2531N6-succinyllysine By similarity
Modified residuei257 – 2571N6-succinyllysine By similarity
Modified residuei393 – 3931N6-succinyllysine By similarity

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDbiP58875.
PRIDEiP58875.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP58875.
SMRiP58875. Positions 1-396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 249174CRAL-TRIO
Add
BLAST
Domaini275 – 383109GOLD
Add
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.
Contains 1 GOLD domain.

Phylogenomic databases

eggNOGiNOG309458.
GeneTreeiENSGT00550000074580.
HOGENOMiHOG000232201.
HOVERGENiHBG055336.
OrthoDBiEOG7N8ZVD.
TreeFamiTF313988.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR009038. GOLD.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
PRINTSiPR00180. CRETINALDHBP.
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF101576. SSF101576. 1 hit.
SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P58875-1 [UniParc]FASTAAdd to Basket

« Hide

MSGRVGDLSP KQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARNFNLQ    50
KSEAMLRKHV EFRKQKDIDN IMSWQPPEVV QQYLSGGMCG YDLEGSPIWY 100
DIIGPLDAKG LLLSASKQDL FKTKMRDCEL LLQECVRQTE KMGKKIEATT 150
LIYDCEGLGL KHLWKPAVEA YGEFLCMFEE NYPETLKRLF IVKAPKLFPV 200
AYNLVKPFLS EDTRKKIQVL GANWKEVLLK YISPDQLPVE YGGTMTDPDG 250
NPKCKSKINY GGDIPKKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG 300
CVLRWQFMSD GSDIGFGIFL KTKVGERQRA GEMREVLPSQ RYNAHLVPED 350
GSLTCSDPGI YVLRFDNTYS FIHAKKVSFT VEVLLPDKAL EEKMQQLGAV 400
TPK 403
Length:403
Mass (Da):46,200
Last modified:June 13, 2006 - v2
Checksum:i67C28EFC173E1CD9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931K → G AA sequence 1 Publication
Sequence conflicti343 – 3431N → S in AAL90886. 1 Publication
Sequence conflicti382 – 3821E → D in AAL90886. 1 Publication
Sequence conflicti390 – 3901L → S in AAI09892. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF432353 mRNA. Translation: AAO31942.1.
BC109891 mRNA. Translation: AAI09892.1.
AF487977 mRNA. Translation: AAL90886.1.
RefSeqiNP_808812.2. NM_177943.2.
UniGeneiBt.44611.

Genome annotation databases

EnsembliENSBTAT00000056675; ENSBTAP00000051657; ENSBTAG00000017404.
GeneIDi282469.
KEGGibta:282469.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF432353 mRNA. Translation: AAO31942.1 .
BC109891 mRNA. Translation: AAI09892.1 .
AF487977 mRNA. Translation: AAL90886.1 .
RefSeqi NP_808812.2. NM_177943.2.
UniGenei Bt.44611.

3D structure databases

ProteinModelPortali P58875.
SMRi P58875. Positions 1-396.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P58875.
PRIDEi P58875.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000056675 ; ENSBTAP00000051657 ; ENSBTAG00000017404 .
GeneIDi 282469.
KEGGi bta:282469.

Organism-specific databases

CTDi 23541.

Phylogenomic databases

eggNOGi NOG309458.
GeneTreei ENSGT00550000074580.
HOGENOMi HOG000232201.
HOVERGENi HBG055336.
OrthoDBi EOG7N8ZVD.
TreeFami TF313988.

Miscellaneous databases

NextBioi 20806234.

Family and domain databases

Gene3Di 3.40.525.10. 1 hit.
InterProi IPR001071. CRAL-bd_toc_tran.
IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
IPR009038. GOLD.
[Graphical view ]
Pfami PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view ]
PRINTSi PR00180. CRETINALDHBP.
SMARTi SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF101576. SSF101576. 1 hit.
SSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
PS50866. GOLD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 178-195 AND 335-353.
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "Induction of hepatic tocopherol associated protein (TAP) mRNA but not alpha-tocopherol transfer protein (TTP) mRNA in cattle fed increasing levels of vitamin E."
    Meadus J., MacInnis R., Dubeski P., Hidiroglou N., Madere R.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-387.
    Tissue: Liver.

Entry informationi

Entry nameiS14L2_BOVIN
AccessioniPrimary (citable) accession number: P58875
Secondary accession number(s): Q32KW6, Q867A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 13, 2006
Last modified: March 19, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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