OSBL1_HUMAN
ID OSBL1_HUMAN Reviewed; 950 AA.
AC Q9BXW6; B7Z7D3; Q9BZF5; Q9NW87;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Oxysterol-binding protein-related protein 1;
DE Short=ORP-1;
DE Short=OSBP-related protein 1;
GN Name=OSBPL1A; Synonyms=ORP1, OSBP8, OSBPL1, OSBPL1B;
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] (ISOFORMS A AND B), AND VARIANT PRO-810.
RX PubMed=11735225; DOI=10.1006/geno.2001.6663;
RA Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
RT "A family of 12 human genes containing oxysterol-binding domains.";
RL Genomics 78:185-196(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=11279184; DOI=10.1074/jbc.m101204200;
RA Xu Y., Liu Y., Ridgway N.D., McMaster C.R.;
RT "Novel members of the human oxysterol-binding protein family bind
RT phospholipids and regulate vesicle transport.";
RL J. Biol. Chem. 276:18407-18414(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND GENE FAMILY.
RX PubMed=11483621;
RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B.,
RA Ikonen E., Olkkonen V.M.;
RT "The OSBP-related protein family in humans.";
RL J. Lipid Res. 42:1203-1213(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 514-790 (ISOFORM A).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB7A.
RX PubMed=16176980; DOI=10.1091/mbc.e05-03-0189;
RA Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
RT "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
RT alters functional properties of late endocytic compartments.";
RL Mol. Biol. Cell 16:5480-5492(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION.
RX PubMed=17428193; DOI=10.1042/bj20070176;
RA Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H.,
RA Radzikowska A., Thiele C., Olkkonen V.M.;
RT "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-
RT hydroxycholesterol in an evolutionarily conserved pocket.";
RL Biochem. J. 405:473-480(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MOSPD2, SUBCELLULAR
RP LOCATION, DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF 476-PHE--TYR-477.
RX PubMed=29858488; DOI=10.15252/embr.201745453;
RA Di Mattia T., Wilhelm L.P., Ikhlef S., Wendling C., Spehner D., Nomine Y.,
RA Giordano F., Mathelin C., Drin G., Tomasetto C., Alpy F.;
RT "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum
RT membrane contact sites.";
RL EMBO Rep. 19:0-0(2018).
CC -!- FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic
CC acid and weak binding to phosphatidylinositol 3-phosphate (By
CC similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and
CC alters functional properties of late endocytic compartments via its
CC interaction with RAB7A (PubMed:16176980). Binds 25-hydroxycholesterol
CC and cholesterol (PubMed:17428193). {ECO:0000250,
CC ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17428193}.
CC -!- SUBUNIT: Interacts with VAPA (By similarity). Interacts with the GTP-
CC bound form of RAB7A (PubMed:17081983). Interacts with OAS1B (By
CC similarity). Interacts (via FFAT motif) with MOSPD2 (via MSP domain)
CC (PubMed:29858488). {ECO:0000250|UniProtKB:Q8K4M9,
CC ECO:0000250|UniProtKB:Q91XL9, ECO:0000269|PubMed:17081983,
CC ECO:0000269|PubMed:29858488}.
CC -!- INTERACTION:
CC Q9BXW6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-765918, EBI-16439278;
CC Q9BXW6; Q8NHP6: MOSPD2; NbExp=8; IntAct=EBI-765918, EBI-2812848;
CC Q9BXW6; P51149: RAB7A; NbExp=5; IntAct=EBI-765918, EBI-1056089;
CC Q9BXW6; Q9P0L0: VAPA; NbExp=4; IntAct=EBI-765918, EBI-1059156;
CC Q9BXW6; O95292: VAPB; NbExp=5; IntAct=EBI-765918, EBI-1188298;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:16176980,
CC ECO:0000269|PubMed:29858488}. Note=Colocalizes with RAB7A, RAB9A and
CC LAMP1 in late endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B; Synonyms=OSBPL1B, OSBP8L, ORP1L;
CC IsoId=Q9BXW6-1; Sequence=Displayed;
CC Name=A; Synonyms=OSBPL1A, OSBP8S;
CC IsoId=Q9BXW6-2; Sequence=VSP_003779;
CC Name=4;
CC IsoId=Q9BXW6-4; Sequence=VSP_045443;
CC -!- DOMAIN: The FFAT motif is required for interaction with MOSPD2.
CC {ECO:0000269|PubMed:29858488}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53407.2; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF392449; AAL40662.1; -; mRNA.
DR EMBL; AF392450; AAL40663.1; -; mRNA.
DR EMBL; AF274714; AAK15154.1; -; mRNA.
DR EMBL; AF323726; AAG53407.2; ALT_SEQ; mRNA.
DR EMBL; AK001079; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK301862; BAH13569.1; -; mRNA.
DR EMBL; AC023983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11884.1; -. [Q9BXW6-1]
DR CCDS; CCDS11885.1; -. [Q9BXW6-2]
DR CCDS; CCDS56056.1; -. [Q9BXW6-4]
DR RefSeq; NP_001229437.1; NM_001242508.1. [Q9BXW6-4]
DR RefSeq; NP_060500.3; NM_018030.4. [Q9BXW6-2]
DR RefSeq; NP_542164.2; NM_080597.3. [Q9BXW6-1]
DR RefSeq; XP_016881022.1; XM_017025533.1. [Q9BXW6-2]
DR RefSeq; XP_016881023.1; XM_017025534.1.
DR PDB; 5ZM5; X-ray; 2.60 A; A=534-950.
DR PDB; 5ZM6; X-ray; 2.70 A; A/B=524-950.
DR PDB; 5ZM7; X-ray; 3.40 A; A=524-950.
DR PDB; 6IYB; X-ray; 2.09 A; B/D=5-152.
DR PDB; 6TQS; X-ray; 2.25 A; G/H/I/J/K=469-485.
DR PDBsum; 5ZM5; -.
DR PDBsum; 5ZM6; -.
DR PDBsum; 5ZM7; -.
DR PDBsum; 6IYB; -.
DR PDBsum; 6TQS; -.
DR AlphaFoldDB; Q9BXW6; -.
DR SMR; Q9BXW6; -.
DR BioGRID; 125379; 38.
DR IntAct; Q9BXW6; 24.
DR MINT; Q9BXW6; -.
DR STRING; 9606.ENSP00000320291; -.
DR SwissLipids; SLP:000001534; -.
DR iPTMnet; Q9BXW6; -.
DR PhosphoSitePlus; Q9BXW6; -.
DR BioMuta; OSBPL1A; -.
DR DMDM; 20143880; -.
DR EPD; Q9BXW6; -.
DR jPOST; Q9BXW6; -.
DR MassIVE; Q9BXW6; -.
DR MaxQB; Q9BXW6; -.
DR PaxDb; Q9BXW6; -.
DR PeptideAtlas; Q9BXW6; -.
DR PRIDE; Q9BXW6; -.
DR ProteomicsDB; 6854; -.
DR ProteomicsDB; 79527; -. [Q9BXW6-1]
DR ProteomicsDB; 79528; -. [Q9BXW6-2]
DR Antibodypedia; 22086; 193 antibodies from 29 providers.
DR DNASU; 114876; -.
DR Ensembl; ENST00000319481.8; ENSP00000320291.3; ENSG00000141447.19. [Q9BXW6-1]
DR Ensembl; ENST00000357041.8; ENSP00000349545.4; ENSG00000141447.19. [Q9BXW6-4]
DR Ensembl; ENST00000399443.7; ENSP00000382372.3; ENSG00000141447.19. [Q9BXW6-2]
DR GeneID; 114876; -.
DR KEGG; hsa:114876; -.
DR MANE-Select; ENST00000319481.8; ENSP00000320291.3; NM_080597.4; NP_542164.2.
DR UCSC; uc002kvd.5; human. [Q9BXW6-1]
DR CTD; 114876; -.
DR DisGeNET; 114876; -.
DR GeneCards; OSBPL1A; -.
DR HGNC; HGNC:16398; OSBPL1A.
DR HPA; ENSG00000141447; Low tissue specificity.
DR MIM; 606730; gene.
DR neXtProt; NX_Q9BXW6; -.
DR OpenTargets; ENSG00000141447; -.
DR PharmGKB; PA32826; -.
DR VEuPathDB; HostDB:ENSG00000141447; -.
DR eggNOG; KOG2209; Eukaryota.
DR GeneTree; ENSGT00940000155295; -.
DR HOGENOM; CLU_007105_5_1_1; -.
DR InParanoid; Q9BXW6; -.
DR OMA; AQTCQQK; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q9BXW6; -.
DR TreeFam; TF320922; -.
DR PathwayCommons; Q9BXW6; -.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SignaLink; Q9BXW6; -.
DR BioGRID-ORCS; 114876; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; OSBPL1A; human.
DR GeneWiki; OSBPL1A; -.
DR GenomeRNAi; 114876; -.
DR Pharos; Q9BXW6; Tbio.
DR PRO; PR:Q9BXW6; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9BXW6; protein.
DR Bgee; ENSG00000141447; Expressed in corpus callosum and 201 other tissues.
DR ExpressionAtlas; Q9BXW6; baseline and differential.
DR Genevisible; Q9BXW6; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; NAS:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Coiled coil; Endosome;
KW Lipid transport; Lipid-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..950
FT /note="Oxysterol-binding protein-related protein 1"
FT /id="PRO_0000100367"
FT REPEAT 47..76
FT /note="ANK 1"
FT REPEAT 80..109
FT /note="ANK 2"
FT REPEAT 175..204
FT /note="ANK 3"
FT DOMAIN 235..334
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..237
FT /note="Interaction with RAB7A"
FT /evidence="ECO:0000269|PubMed:16176980"
FT REGION 501..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..463
FT /evidence="ECO:0000255"
FT COILED 877..913
FT /evidence="ECO:0000255"
FT MOTIF 469..483
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:29858488"
FT COMPBIAS 501..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..513
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11279184,
FT ECO:0000303|PubMed:11735225, ECO:0000303|PubMed:14702039"
FT /id="VSP_003779"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045443"
FT VARIANT 810
FT /note="S -> P (in dbSNP:rs35693789)"
FT /evidence="ECO:0000269|PubMed:11735225"
FT /id="VAR_053547"
FT MUTAGEN 476..477
FT /note="FY->AA: Loss of interaction with MOSPD2."
FT /evidence="ECO:0000269|PubMed:29858488"
FT CONFLICT 735
FT /note="T -> A (in Ref. 4; AK001079)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="P -> S (in Ref. 1; AAL40662)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="A -> G (in Ref. 1; AAL40662)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:6IYB"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6IYB"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6IYB"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:6IYB"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:5ZM6"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 571..575
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 576..581
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 588..594
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 599..613
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 632..637
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 642..650
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 651..654
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 655..662
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 665..680
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 709..718
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 721..732
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 751..754
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 755..761
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 767..774
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 775..777
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 778..782
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 784..792
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 831..835
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 846..848
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 851..856
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 861..864
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 876..882
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 886..909
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 917..923
FT /evidence="ECO:0007829|PDB:5ZM5"
FT TURN 925..927
FT /evidence="ECO:0007829|PDB:5ZM5"
FT STRAND 930..934
FT /evidence="ECO:0007829|PDB:5ZM5"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:5ZM5"
SQ SEQUENCE 950 AA; 108470 MW; CDDA26CA27B65F63 CRC64;
MNTEAEQQLL HHARNGNAEE VRQLLETMAR NEVIADINCK GRSKSNLGWT PLHLACYFGH
RQVVQDLLKA GAEVNVLNDM GDTPLHRAAF TGRKELVMLL LEYNADTTIV NGSGQTAKEV
THAEEIRSML EAVERTQQRK LEELLLAAAR EGKTTELTAL LNRPNPPDVN CSDQLGNTPL
HCAAYRAHKQ CALKLLRSGA DPNLKNKNDQ KPLDLAQGAE MKHILVGNKV IYKALKRYEG
PLWKSSRFFG WRLFWVVLEH GVLSWYRKQP DAVHNIYRQG CKHLTQAVCT VKSTDSCLFF
IKCFDDTIHG FRVPKNSLQQ SREDWLEAIE EHSAYSTHYC SQDQLTDEEE EDTVSAADLK
KSLEKAQSCQ QRLDREISNF LKMIKECDMA KEMLPSFLQK VEVVSEASRE TCVALTDCLN
LFTKQEGVRN FKLEQEQEKN KILSEALETL ATEHHELEQS LVKGSPPASI LSEDEFYDAL
SDSESERSLS RLEAVTARSF EEEGEHLGSR KHRMSEEKDC GGGDALSNGI KKHRTSLPSP
MFSRNDFSIW SILRKCIGME LSKITMPVIF NEPLSFLQRL TEYMEHTYLI HKASSLSDPV
ERMQCVAAFA VSAVASQWER TGKPFNPLLG ETYELVRDDL GFRLISEQVS HHPPISAFHA
EGLNNDFIFH GSIYPKLKFW GKSVEAEPKG TITLELLEHN EAYTWTNPTC CVHNIIVGKL
WIEQYGNVEI INHKTGDKCV LNFKPCGLFG KELHKVEGYI QDKSKKKLCA LYGKWTECLY
SVDPATFDAY KKNDKKNTEE KKNSKQMSTS EELDEMPVPD SESVFIIPGS VLLWRIAPRP
PNSAQMYNFT SFAMVLNEVD KDMESVIPKT DCRLRPDIRA MENGEIDQAS EEKKRLEEKQ
RAARKNRSKS EEDWKTRWFH QGPNPYNGAQ DWIYSGSYWD RNYFNLPDIY
