ID L9KGM3_TUPCH Unreviewed; 1829 AA.
AC L9KGM3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
DE Flags: Fragment;
GN ORFNames=TREES_T100009169 {ECO:0000313|EMBL:ELW61619.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW61619.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|RuleBase:RU003844}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL33 family.
CC {ECO:0000256|ARBA:ARBA00009269}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KB320867; ELW61619.1; -; Genomic_DNA.
DR STRING; 246437.L9KGM3; -.
DR MEROPS; M08.003; -.
DR eggNOG; KOG2210; Eukaryota.
DR InParanoid; L9KGM3; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd07622; BAR_SNX4; 1.
DR CDD; cd13291; PH_ORP10_ORP11; 1.
DR CDD; cd06864; PX_SNX4; 1.
DR Gene3D; 1.10.287.2720; -; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 6.10.140.1150; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.10.55.10; Leishmanolysin domain 3; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.40.10.190; translation elongation factor selb, chain A, domain 4; 1.
DR HAMAP; MF_00573; Ribosomal_L35Ae; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR001577; Peptidase_M8.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034902; PX_SNX4.
DR InterPro; IPR001780; Ribosomal_eL33.
DR InterPro; IPR018266; Ribosomal_eL33_CS.
DR InterPro; IPR038661; Ribosomal_eL33_sf.
DR InterPro; IPR034783; SNX4.
DR InterPro; IPR037430; SNX4_BAR.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR46596; SORTING NEXIN-4; 1.
DR PANTHER; PTHR46596:SF1; SORTING NEXIN-4; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF01247; Ribosomal_L35Ae; 1.
DR PRINTS; PR00782; LSHMANOLYSIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS01105; RIBOSOMAL_L35AE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU003845};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 801..877
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1403..1529
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 646..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1778..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1781..1795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELW61619.1"
SQ SEQUENCE 1829 AA; 207716 MW; 9DD7F6A1C31A84FD CRC64;
RLWSKAIFAG YKRGLRNQRE HTALLKIEGV YARDETEFYL GKRCAYVYKA KNNTVTPGGK
PNKTRVIWGK VTRAHGNSGM VRAKFRSNLP AKAIGHRIRV IINKVHLKAN HVIKRDVDEH
LRIKTVYDKS IEELLPEKRY LVKNKLFPQA ISYLEKTFQV RRPAGTILLS RQCATNQYLR
KENDPHRYCT GECAVHTKCG PVIVPEEHLQ QCRVCRGGKW PCGGVGVQDQ EGVRDADFIL
YVGALATERC SHENIIGFSA GLFAFYHDKD GNPLTSRFAD GLPPFNYSLG LYQWSDKVVR
KVERLWDVRD NKIVRHTVYL LVTPRVVNEA MTGSHTQNRV LSRITLALME DTGWYKANYS
MAEKLDWGRG MGCDFVRKSC KFWIDQQRQK RQMLSPFCDT LRSNPLQLTC RQDQRAVAVC
NLQKFPKPLP QEYQYFDELS GIPAEDLPYY GGSVEIADYC PFSQEFSWHL SGEYQRSSDC
RILENQPEIL KNYGAEKYGP HSVCLIQKSA FVMEKCERKL SYPDWGSGCY QVSCSPQGLK
VWVQDTSYLC SRAGQVLPVS IQMNGWIHGG NLLCPSCGDF CELCPPETDP PAANLTRALP
LGTGKTVLDI PLCHVPVNKA QNLGKRQAVQ VAEAFPTSVW MVDHTQASEQ SSHSSQPSTS
EFGGAEGFPD HQVSSLFKIR NLEGEISFGS GIIGEVFRVI TYLIIFINLR QCEGSSWSKL
NELIIARLEI VDPVFNSSVM MFGKARTNQL HLGEGDAKDS RPHESHQLMD TAQVSFRGKT
NWDVTSGHDH TDVCTEKSSP FFVLNNEAGL LEYFVNEQSR NQKPRGTLQL AGAVISPSDE
DSHTFTVNAA SGEQYKLRAT DAKERQHWVS RLQICTQHHT EAIGKMMSHA EGQQRDLIRR
IECLPTSGHL SSLDQDLLML KATSMATMNC LNDCFHILQL QHASHQKGSL PSGTTIEWLE
PKIPLSNHYK NGADQPFATE QSKPVAVPEE QSVAESGLLA REPEEISAHD EMEDTCDDKE
DDLGAVEEQR SVILHLLSQL KLGMDLTRVV LPTFILEKRS LLEMYADFMS HPDLFLAITN
GATAEDRMIR FVEYYLTSFH EGRKGAIAKK PYNPIIGETF HCSWRVPKSE VACSVASSSP
TPAVTNHAPL SEEALSQADS DCYMVRFVAE QVSHHPPVSG FYAECAERKM CVNAHVWTKS
KFLGMSIGVT MVGEGILSLL EHGEEYTFSL PCAYARSILT VPWVELGGKV SVNCAKTGYS
ASITFHTKPF YGGKLHRVTA EVKHNITNTV VCRVQGEWNS VLEFTYSNGE TKCVDLTKLS
VTKKRVRPLE KQDPFESRRL WKNVTDALRE SEIDKATEHK RSLEERQRTE ERHRTETGTP
WKTQYFIKET TENSFWLKKI EISVSEAEKR TGRNAMNMQE TYTAYLIETR SVEHSDGQSV
LTDSLWRRYS EFELLRNYLL VYYPHIVVPP LPEKRAEFVW HKLSADNMDP DFVERRRIGL
ENFLLRVASH PILCRDKIFY LFLTQEGNWK ETVNETGFQL KADSRLKALN ATFRVKNPDK
RFTELKHYSD ELQAVIAHLL RVRARVADRL YGVYKVHGNY GRVFSEWSAI EKEMGDGLQS
AGHHMDVYAS SIDDILEDEE HYADQLKEYL FYAEALRAVC RKHELMQYDL EMAAQDLASK
KQQCEELATG GMTTKLFGQE TPEQREARIK VLEEQISEGE QQLKSKNSEG REFVKNAWAD
IERFKEQKNH DLKEALISYA VMQISMCKKC SGFLQNKSTE EQEVRNSENR NDTSSPSRRA
RPTGTAMVLQ LTLLSLAAAD LTLRCLFNV
//
