SNX7_MACFA
ID SNX7_MACFA Reviewed; 387 AA.
AC Q4R5U9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Sorting nexin-7;
GN Name=SNX7; ORFNames=QtsA-20671;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking. Together with SNX4, involved in
CC autophagosome assembly by regulating trafficking and recycling of
CC phospholipid scramblase ATG9A. {ECO:0000250|UniProtKB:Q9UNH6}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX4.
CC {ECO:0000250|UniProtKB:Q9UNH6}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9UNH6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95219}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AB169444; BAE01526.1; -; mRNA.
DR AlphaFoldDB; Q4R5U9; -.
DR SMR; Q4R5U9; -.
DR STRING; 9541.XP_005542683.1; -.
DR eggNOG; KOG2273; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR CDD; cd07666; BAR_SNX7; 1.
DR CDD; cd07284; PX_SNX7; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR042131; BAR_SNX7.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042130; PX_SNX7.
DR InterPro; IPR028656; SNX7.
DR PANTHER; PTHR45949:SF3; PTHR45949:SF3; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Endosome; Lipid-binding; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..387
FT /note="Sorting nexin-7"
FT /id="PRO_0000213849"
FT DOMAIN 30..151
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 178..387
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT BINDING 73
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT BINDING 75
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT BINDING 103
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 117
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T1"
SQ SEQUENCE 387 AA; 45324 MW; 2A727F80112D632F CRC64;
MDMNSFSPMM PTSPLSMINQ IKFEDEPDLK DLFITVDEPE SHVTTIETFI TYRIITKTSR
GEFDSSEFEV RRRYQDFLWL KGKLEEAHPT LIIPPLPEKF IVKGMVERFN DDFIETRRKA
LHKFLNRIAD HPTLTFNEDF KIFLTAQAWE LSSHKKQGPG LLSRMGQTVR AVASSMRGVK
NRPEEFMEMN NFIELFSQKI NLIDKISQRI YKEEREYFDE MKEYGPIHIL WSASEEDLVD
TLKDVAGCID RCCKATEKRM SGLSEALLPV VREYVLYSEM LMGVMKRRDQ IQAELDSKVE
ALTYKKTDTD LLPEEIGKLE DKVECANNAL KADWERWKQN MQNDIKLAFT DMAEENIHYY
EQCLATWESF LTSQTNLHLE ETSEDKP