ID G7MQ21_MACMU Unreviewed; 591 AA.
AC G7MQ21;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Sorting nexin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=EGK_15227 {ECO:0000313|EMBL:EHH18585.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH18585.1};
RN [1] {ECO:0000313|EMBL:EHH18585.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH18585.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; CM001256; EHH18585.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MQ21; -.
DR Proteomes; UP000013456; Chromosome 4.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR CDD; cd07668; BAR_SNX9; 1.
DR CDD; cd07285; PX_SNX9; 1.
DR CDD; cd11898; SH3_SNX9; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037425; SNX9_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR037426; SNX9_PX.
DR InterPro; IPR035558; SNX9_SH3.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF2; SORTING NEXIN-9; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT DOMAIN 1..58
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 246..357
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 87..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 284
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 323
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH18585.1"
FT NON_TER 591
FT /evidence="ECO:0000313|EMBL:EHH18585.1"
SQ SEQUENCE 591 AA; 66093 MW; B886C1F79F8B2D94 CRC64;
ARVMYDFAAE PGNNELTVNE GEIITITNPD VGGGWLEGRN IKGERGLVPT DYVEILPSDG
KDQFSCGNSV ADQAFLDSLS ASTAQASSSA ASNNHQVGSG NDPWSAWSAS KSGNWESSEG
WGAQPEGAGA QRSTNTPNNW DTAFGHPQAY QGPATGDDDD WDEDWDGPKS SSYFKDSESA
DAGGSQRGNS RASSSSMKIP LNKFPGFAKP GTEQYLLAKQ LAKPKEKIPI IVGDYGPMWV
YPTSTFDCVV ADPRKGSKMY GLKSYIEYQL TPTNTNRSVN HRYKHFDWLY ERLLVKFGSA
IPIPSLPDKQ VTGRFEEEFI KMRMERLQAW MTRMCRHPVI SESEVFQQFL NFRDEKEWKT
GKRKAEKDEL AGVMIFSTME PEAPDLDLVE IEQKCEAVGK FTKAMDDGVK ELLTVGQEHW
KRCTGPLPKE YQKIGKALQS LATVFSSSGY QGETDLNDAI TEAGKTYEEI ASLVAEQPKK
DLHFLMECNH EYKGFLGCFP DIIGTHKGAI EKVKESDKLV ATSKITPQDK QNMVKRVSTM
SYALQAEMNH FHSNRIYDYN SVIRLYLEQQ VQFYETIAEK LRQALSRFPV M
//
