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S14L3_HUMAN
ID   S14L3_HUMAN             Reviewed;         400 AA.
AC   Q9UDX4; E7EN74; E9PE57; Q495V8; Q495W0; Q495W1;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=SEC14-like protein 3;
DE   AltName: Full=Tocopherol-associated protein 2;
GN   Name=SEC14L3; Synonyms=TAP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 functional
RT   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., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., 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., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., 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., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   THR-103 AND GLU-335.
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).
CC   -!- FUNCTION: Probable hydrophobic ligand-binding protein; may play a role
CC       in the transport of hydrophobic ligands like tocopherol, squalene and
CC       phospholipids.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UDX4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UDX4-2; Sequence=VSP_045554;
CC       Name=3;
CC         IsoId=Q9UDX4-3; Sequence=VSP_045553;
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DR   EMBL; AY158086; AAO21870.1; -; mRNA.
DR   EMBL; AC004832; AAF19258.1; -; Genomic_DNA.
DR   EMBL; BC101001; AAI01002.1; -; mRNA.
DR   EMBL; BC101002; AAI01003.1; -; mRNA.
DR   EMBL; BC101004; AAI01005.1; -; mRNA.
DR   CCDS; CCDS13877.1; -. [Q9UDX4-1]
DR   CCDS; CCDS58800.1; -. [Q9UDX4-3]
DR   CCDS; CCDS58801.1; -. [Q9UDX4-2]
DR   RefSeq; NP_001244307.1; NM_001257378.1. [Q9UDX4-3]
DR   RefSeq; NP_001244308.1; NM_001257379.1. [Q9UDX4-2]
DR   RefSeq; NP_001244311.1; NM_001257382.1. [Q9UDX4-2]
DR   RefSeq; NP_777635.1; NM_174975.4. [Q9UDX4-1]
DR   PDB; 4UYB; X-ray; 1.50 A; A=1-400.
DR   PDBsum; 4UYB; -.
DR   AlphaFoldDB; Q9UDX4; -.
DR   SMR; Q9UDX4; -.
DR   BioGRID; 129297; 6.
DR   IntAct; Q9UDX4; 3.
DR   STRING; 9606.ENSP00000215812; -.
DR   DrugBank; DB14003; alpha-Tocopherol acetate.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR   DrugBank; DB11635; Tocofersolan.
DR   DrugBank; DB11251; Tocopherol.
DR   DrugBank; DB00163; Vitamin E.
DR   iPTMnet; Q9UDX4; -.
DR   PhosphoSitePlus; Q9UDX4; -.
DR   BioMuta; SEC14L3; -.
DR   DMDM; 29428056; -.
DR   EPD; Q9UDX4; -.
DR   jPOST; Q9UDX4; -.
DR   MassIVE; Q9UDX4; -.
DR   MaxQB; Q9UDX4; -.
DR   PaxDb; Q9UDX4; -.
DR   PeptideAtlas; Q9UDX4; -.
DR   PRIDE; Q9UDX4; -.
DR   Antibodypedia; 59073; 47 antibodies from 11 providers.
DR   DNASU; 266629; -.
DR   Ensembl; ENST00000215812.9; ENSP00000215812.5; ENSG00000100012.12. [Q9UDX4-1]
DR   Ensembl; ENST00000401751.5; ENSP00000383896.1; ENSG00000100012.12. [Q9UDX4-2]
DR   Ensembl; ENST00000402286.5; ENSP00000385004.1; ENSG00000100012.12. [Q9UDX4-3]
DR   Ensembl; ENST00000540910.5; ENSP00000439752.1; ENSG00000100012.12. [Q9UDX4-3]
DR   GeneID; 266629; -.
DR   KEGG; hsa:266629; -.
DR   MANE-Select; ENST00000215812.9; ENSP00000215812.5; NM_174975.5; NP_777635.1.
DR   UCSC; uc003ahy.4; human. [Q9UDX4-1]
DR   CTD; 266629; -.
DR   DisGeNET; 266629; -.
DR   GeneCards; SEC14L3; -.
DR   HGNC; HGNC:18655; SEC14L3.
DR   HPA; ENSG00000100012; Tissue enhanced (bone marrow, liver, retina).
DR   MIM; 612824; gene.
DR   neXtProt; NX_Q9UDX4; -.
DR   OpenTargets; ENSG00000100012; -.
DR   PharmGKB; PA134960743; -.
DR   VEuPathDB; HostDB:ENSG00000100012; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   GeneTree; ENSGT00940000162077; -.
DR   HOGENOM; CLU_014001_2_1_1; -.
DR   InParanoid; Q9UDX4; -.
DR   OMA; VYIEQMG; -.
DR   PhylomeDB; Q9UDX4; -.
DR   TreeFam; TF313988; -.
DR   PathwayCommons; Q9UDX4; -.
DR   SignaLink; Q9UDX4; -.
DR   BioGRID-ORCS; 266629; 10 hits in 1066 CRISPR screens.
DR   GenomeRNAi; 266629; -.
DR   Pharos; Q9UDX4; Tbio.
DR   PRO; PR:Q9UDX4; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9UDX4; protein.
DR   Bgee; ENSG00000100012; Expressed in olfactory segment of nasal mucosa and 36 other tissues.
DR   ExpressionAtlas; Q9UDX4; baseline and differential.
DR   Genevisible; Q9UDX4; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
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   3D-structure; Alternative splicing; Lipid-binding; Reference proteome;
KW   Transport.
FT   CHAIN           1..400
FT                   /note="SEC14-like protein 3"
FT                   /id="PRO_0000210758"
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   VAR_SEQ         1..78
FT                   /note="MSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKS
FT                   EALLRKYMEFRKTMDIDHILDWQPPE -> M (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045553"
FT   VAR_SEQ         1..59
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045554"
FT   VARIANT         103
FT                   /note="I -> T (in dbSNP:rs4820853)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_024627"
FT   VARIANT         214
FT                   /note="R -> H (in dbSNP:rs2269961)"
FT                   /id="VAR_024628"
FT   VARIANT         335
FT                   /note="D -> E (in dbSNP:rs2240345)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022097"
FT   VARIANT         364
FT                   /note="R -> C (in dbSNP:rs35764129)"
FT                   /id="VAR_061787"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           35..44
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           49..65
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           68..73
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           78..83
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           108..112
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           117..142
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           165..181
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          186..193
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           198..205
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           211..215
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           224..231
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          279..285
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          289..296
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          302..308
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          314..324
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           330..332
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          333..342
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          349..354
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          359..366
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   STRAND          371..384
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           388..391
FT                   /evidence="ECO:0007829|PDB:4UYB"
FT   HELIX           392..396
FT                   /evidence="ECO:0007829|PDB:4UYB"
SQ   SEQUENCE   400 AA;  46048 MW;  07F880D25B66CC19 CRC64;
     MSGRVGDLSP KQAETLAKFR ENVQDVLPAL PNPDDYFLLR WLRARNFDLQ KSEALLRKYM
     EFRKTMDIDH ILDWQPPEVI QKYMPGGLCG YDRDGCPVWY DIIGPLDPKG LLFSVTKQDL
     LKTKMRDCER ILHECDLQTE RLGKKIETIV MIFDCEGLGL KHFWKPLVEV YQEFFGLLEE
     NYPETLKFML IVKATKLFPV GYNLMKPFLS EDTRRKIIVL GNNWKEGLLK LISPEELPAQ
     FGGTLTDPDG NPKCLTKINY GGEIPKSMYV RDQVKTQYEH SVQINRGSSH QVEYEILFPG
     CVLRWQFSSD GADIGFGVFL KTKMGERQRA GEMTDVLPSQ RYNAHMVPED GNLTCSEAGV
     YVLRFDNTYS FVHAKKVSFT VEVLLPDEGM QKYDKELTPV
 
 
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