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APOF_HUMAN
ID   APOF_HUMAN              Reviewed;         326 AA.
AC   Q13790; Q8TC13;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Apolipoprotein F;
DE            Short=Apo-F;
DE   AltName: Full=Lipid transfer inhibitor protein;
DE            Short=LTIP;
DE   Flags: Precursor;
GN   Name=APOF;
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], PROTEIN SEQUENCE OF 165-194 AND 251-265,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hepatoma;
RX   PubMed=8093033; DOI=10.1006/bbrc.1994.2302;
RA   Day J.R., Albers J.J., Gilbert T.L., Whitmore T.E., McConathy W.J.,
RA   Wolfbauer G.;
RT   "Purification and molecular cloning of human apolipoprotein F.";
RL   Biochem. Biophys. Res. Commun. 203:1146-1151(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 165-178, AND FUNCTION.
RC   TISSUE=Liver, and Plasma;
RX   PubMed=9880564; DOI=10.1074/jbc.274.3.1814;
RA   Wang X., Driscoll D.M., Morton R.E.;
RT   "Molecular cloning and expression of lipid transfer inhibitor protein
RT   reveals its identity with apolipoprotein F.";
RL   J. Biol. Chem. 274:1814-1820(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=204339; DOI=10.1021/bi00599a014;
RA   Olofsson S.-O., McConathy W.J., Alaupovic P.;
RT   "Isolation and partial characterization of a new acidic apolipoprotein
RT   (apolipoprotein F) from high density lipoproteins of human plasma.";
RL   Biochemistry 17:1032-1036(1978).
RN   [6]
RP   GLYCOSYLATION AT THR-274, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-323, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=28935895; DOI=10.1038/s41598-017-12229-2;
RA   Kumar A., Gangadharan B., Cobbold J., Thursz M., Zitzmann N.;
RT   "Absolute quantitation of disease protein biomarkers in a single LC-MS
RT   acquisition using apolipoprotein F as an example.";
RL   Sci. Rep. 7:12072-12072(2017).
CC   -!- FUNCTION: Minor apolipoprotein that associates with LDL. Inhibits
CC       cholesteryl ester transfer protein (CETP) activity and appears to be an
CC       important regulator of cholesterol transport. Also associates to a
CC       lesser degree with VLDL, Apo-AI and Apo-AII.
CC       {ECO:0000269|PubMed:9880564}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:204339,
CC       ECO:0000269|PubMed:28935895, ECO:0000269|PubMed:8093033}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC       {ECO:0000269|PubMed:8093033}.
CC   -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC       {ECO:0000269|PubMed:22171320}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein F family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; L27050; AAA65642.1; -; mRNA.
DR   EMBL; AC025574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026257; AAH26257.1; -; mRNA.
DR   CCDS; CCDS44923.1; -.
DR   PIR; JC2549; JC2549.
DR   RefSeq; NP_001629.1; NM_001638.2.
DR   AlphaFoldDB; Q13790; -.
DR   BioGRID; 106816; 4.
DR   IntAct; Q13790; 1.
DR   STRING; 9606.ENSP00000381250; -.
DR   GlyConnect; 702; 16 N-Linked glycans (3 sites), 1 O-Linked glycan (1 site).
DR   GlyGen; Q13790; 8 sites, 16 N-linked glycans (3 sites), 6 O-linked glycans (5 sites).
DR   iPTMnet; Q13790; -.
DR   PhosphoSitePlus; Q13790; -.
DR   BioMuta; APOF; -.
DR   DMDM; 327478500; -.
DR   jPOST; Q13790; -.
DR   MassIVE; Q13790; -.
DR   PaxDb; Q13790; -.
DR   PeptideAtlas; Q13790; -.
DR   PRIDE; Q13790; -.
DR   ProteomicsDB; 59683; -.
DR   Antibodypedia; 28188; 300 antibodies from 34 providers.
DR   DNASU; 319; -.
DR   Ensembl; ENST00000398189.4; ENSP00000381250.3; ENSG00000175336.10.
DR   GeneID; 319; -.
DR   KEGG; hsa:319; -.
DR   MANE-Select; ENST00000398189.4; ENSP00000381250.3; NM_001638.4; NP_001629.1.
DR   UCSC; uc001sle.2; human.
DR   CTD; 319; -.
DR   DisGeNET; 319; -.
DR   GeneCards; APOF; -.
DR   HGNC; HGNC:615; APOF.
DR   HPA; ENSG00000175336; Tissue enriched (liver).
DR   MIM; 107760; gene.
DR   neXtProt; NX_Q13790; -.
DR   OpenTargets; ENSG00000175336; -.
DR   PharmGKB; PA24902; -.
DR   VEuPathDB; HostDB:ENSG00000175336; -.
DR   eggNOG; ENOG502QUQ0; Eukaryota.
DR   GeneTree; ENSGT00500000045104; -.
DR   HOGENOM; CLU_078958_0_0_1; -.
DR   InParanoid; Q13790; -.
DR   OMA; PGFTHMA; -.
DR   OrthoDB; 1568974at2759; -.
DR   PhylomeDB; Q13790; -.
DR   TreeFam; TF338778; -.
DR   PathwayCommons; Q13790; -.
DR   Reactome; R-HSA-8964041; LDL remodeling.
DR   SignaLink; Q13790; -.
DR   BioGRID-ORCS; 319; 8 hits in 1067 CRISPR screens.
DR   GeneWiki; APOF; -.
DR   GenomeRNAi; 319; -.
DR   Pharos; Q13790; Tbio.
DR   PRO; PR:Q13790; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q13790; protein.
DR   Bgee; ENSG00000175336; Expressed in right lobe of liver and 43 other tissues.
DR   Genevisible; Q13790; HS.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0015485; F:cholesterol binding; TAS:ProtInc.
DR   GO; GO:0005319; F:lipid transporter activity; TAS:ProtInc.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR   GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:0006869; P:lipid transport; TAS:ProtInc.
DR   InterPro; IPR026114; APOF.
DR   PANTHER; PTHR15011; PTHR15011; 1.
DR   Pfam; PF15148; Apolipo_F; 1.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Direct protein sequencing; Glycoprotein; HDL; LDL;
KW   Lipid metabolism; Lipid transport; Phosphoprotein; Reference proteome;
KW   Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   PROPEP          36..164
FT                   /evidence="ECO:0000269|PubMed:8093033,
FT                   ECO:0000269|PubMed:9880564"
FT                   /id="PRO_0000002051"
FT   CHAIN           165..326
FT                   /note="Apolipoprotein F"
FT                   /id="PRO_0000002052"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:28935895,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320"
FT   VARIANT         178
FT                   /note="A -> G (in dbSNP:rs11575216)"
FT                   /id="VAR_055520"
SQ   SEQUENCE   326 AA;  35399 MW;  046A1E775E7D4320 CRC64;
     MTGLCGYSAP DMRGLRLIMI PVELLLCYLL LHPVDATSYG KQTNVLMHFP LSLESQTPSS
     DPLSCQFLHP KSLPGFSHMA PLPKFLVSLA LRNALEEAGC QADVWALQLQ LYRQGGVNAT
     QVLIQHLRGL QKGRSTERNV SVEALASALQ LLAREQQSTG RVGRSLPTED CENEKEQAVH
     NVVQLLPGVG TFYNLGTALY YATQNCLGKA RERGRDGAID LGYDLLMTMA GMSGGPMGLA
     ISAALKPALR SGVQQLIQYY QDQKDANISQ PETTKEGLRA ISDVSDLEET TTLASFISEV
     VSSAPYWGWA IIKSYDLDPG AGSLEI
 
 
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