LOCUS       NP_002547                807 aa            linear   PRI 27-APR-2025
DEFINITION  oxysterol-binding protein 1 [Homo sapiens].
ACCESSION   NP_002547
VERSION     NP_002547.1
DBSOURCE    REFSEQ: accession NM_002556.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Lin,Y., Ran,L., Du,X., Yang,H. and Wu,Y.
  TITLE     Oxysterol-Binding Protein: new insights into lipid transport
            functions and human diseases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1868 (9), 159365 (2023)
   PUBMED   37455011
  REMARK    GeneRIF: Oxysterol-Binding Protein: new insights into lipid
            transport functions and human diseases.
            Review article
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Peresse,T., Kovacs,D., Subra,M., Bigay,J., Tsai,M.C., Polidori,J.,
            Gautier,R., Desrat,S., Fleuriot,L., Debayle,D., Litaudon,M.,
            Pham,V.C., Bignon,J., Antonny,B., Roussi,F. and Mesmin,B.
  TITLE     Molecular and cellular dissection of the oxysterol-binding protein
            cycle through a fluorescent inhibitor
  JOURNAL   J Biol Chem 295 (13), 4277-4288 (2020)
   PUBMED   32075908
  REMARK    GeneRIF: Molecular and cellular dissection of the oxysterol-binding
            protein cycle through a fluorescent inhibitor.
REFERENCE   6  (residues 1 to 807)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   7  (residues 1 to 807)
  AUTHORS   Moreira,E.F., Jaworski,C., Li,A. and Rodriguez,I.R.
  TITLE     Molecular and biochemical characterization of a novel
            oxysterol-binding protein (OSBP2) highly expressed in retina
  JOURNAL   J Biol Chem 276 (21), 18570-18578 (2001)
   PUBMED   11278871
REFERENCE   8  (residues 1 to 807)
  AUTHORS   Laitinen,S., Olkkonen,V.M., Ehnholm,C. and Ikonen,E.
  TITLE     Family of human oxysterol binding protein (OSBP) homologues. A
            novel member implicated in brain sterol metabolism
  JOURNAL   J Lipid Res 40 (12), 2204-2211 (1999)
   PUBMED   10588946
REFERENCE   9  (residues 1 to 807)
  AUTHORS   Ridgway,N.D., Dawson,P.A., Ho,Y.K., Brown,M.S. and Goldstein,J.L.
  TITLE     Translocation of oxysterol binding protein to Golgi apparatus
            triggered by ligand binding
  JOURNAL   J Cell Biol 116 (2), 307-319 (1992)
   PUBMED   1730758
REFERENCE   10 (residues 1 to 807)
  AUTHORS   Levanon,D., Hsieh,C.L., Francke,U., Dawson,P.A., Ridgway,N.D.,
            Brown,M.S. and Goldstein,J.L.
  TITLE     cDNA cloning of human oxysterol-binding protein and localization of
            the gene to human chromosome 11 and mouse chromosome 19
  JOURNAL   Genomics 7 (1), 65-74 (1990)
   PUBMED   1970801
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF185696.1 and AP000442.6.
            
            Summary: Oxysterol binding protein is an intracellular protein that
            is believed to transport sterols from lysosomes to the nucleus
            where the sterol down-regulates the genes for the LDL receptor,
            HMG-CoA reductase, and HMG synthetase [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF185696.1, SRR1803617.223496.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263847.6/ ENSP00000263847.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..807
                     /product="oxysterol-binding protein 1"
                     /calculated_mol_wt=89290
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          61..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Region          91..189
                     /region_name="PH_OSBP_ORP4"
                     /note="Human Oxysterol binding protein and OSBP-related
                     protein 4 Pleckstrin homology (PH) domain; cd13284"
                     /db_xref="CDD:270101"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          329..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3B7Z2; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Region          358..364
                     /region_name="FFAT. /evidence=ECO:0000269|PubMed:24209621"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          418..796
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          710..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     CDS             1..807
                     /gene="OSBP"
                     /gene_synonym="OSBP1"
                     /coded_by="NM_002556.3:111..2534"
                     /db_xref="CCDS:CCDS7974.1"
                     /db_xref="GeneID:5007"
                     /db_xref="HGNC:HGNC:8503"
                     /db_xref="MIM:167040"
ORIGIN      
        1 maatelrgvv gpgpaaiaal ggggagppvv gggggrgdag pgsgaasgtv vaaaaggpgp
       61 gaggvaaagp apapptggsg gsgaggsgsa regwlfkwtn yikgyqrrwf vlsngllsyy
      121 rskaemrhtc rgtinlatan itvedscnfi isnggaqtyh lkasseverq rwvtalelak
      181 akavkmlaes desgdeesvs qtdktelqnt lrtlsskved lstcndliak hgtalqrsls
      241 eleslklpae snekikqvne ratlfritsn aminacrdfl mlaqthskkw qkslqyerdq
      301 rirleetleq lakqhnhler afrgatvlpa ntpgnvgsgk dqccsgkgdm sdeddeneff
      361 dapeiitmpe nlghkrtgsn isgassdisl deqykhqlee tkkekrtrip ykpnyslnlw
      421 simkncigke lskipmpvnf neplsmlqrl tedleyhell draakcensl eqlcyvaaft
      481 vssysttvfr tskpfnpllg etfeldrlee ngyrslceqv shhppaaahh aeskngwtlr
      541 qeikitskfr gkylsimplg tihcifhatg hhytwkkvtt tvhniivgkl widqsgeidi
      601 vnhktgdkcn lkfvpysyfs rdvarkvtge vtdpsgkvhf allgtwdekm ecfkvqpvig
      661 enggdarqrg heaeesrvml wkrnplpkna enmyyfsela ltlnawesgt aptdsrlrpd
      721 qrlmengrwd eanaekqrle ekqrlsrkkr eaeamkated gtpydpykal wferkkdpvt
      781 kelthiyrge yweckekqdw sscpdif
//
