SNX27_BOVIN
ID SNX27_BOVIN Reviewed; 541 AA.
AC A5PKA5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sorting nexin-27;
GN Name=SNX27;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the retrograde transport from endosome to plasma
CC membrane, a trafficking pathway that promotes the recycling of
CC internalized transmembrane proteins. Following internalization,
CC endocytosed transmembrane proteins are delivered to early endosomes and
CC recycled to the plasma membrane instead of being degraded in lysosomes.
CC SNX27 specifically binds and directs sorting of a subset of
CC transmembrane proteins containing a PDZ-binding motif at the C-
CC terminus: following interaction with target transmembrane proteins,
CC associates with the retromer complex, preventing entry into the
CC lysosomal pathway, and promotes retromer-tubule based plasma membrane
CC recycling. SNX27 also binds with the WASH complex. Interacts with
CC membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May
CC participate in establishment of natural killer cell polarity. Recruits
CC CYTIP to early endosomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Core component of the SNX27-retromer, a multiprotein complex
CC composed of SNX27, the WASH complex and the retromer complex. Interacts
CC (via PDZ domain) with a number of target transmembrane proteins (via
CC PDZ-binding motif): ABCC4, ADRB2, ARHGEF7, GRIA1, GRIA2, GRIN1, GRIN2A
CC GRIN2C, KCNJ6, KCNJ9 and SLC2A1/GLUT1. Interacts (via the FERM-like
CC regions) with the WASH complex. Interacts with SNX1. Interacts with
CC CYTIP. Interacts with DGKZ. Interacts with MCC (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC Note=Localizes to immunological synapse in T-cells. In T-cells,
CC recruited from the cytosol to sorting endosomes by phosphoinositide-3-
CC kinase products (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain mediates binding to a subset of proteins
CC containing a PDZ-binding motif at the C-terminus: the specificity for
CC PDZ-binding motif is provided by the 2 residues located upstream of the
CC canonical PDZ-binding motif. The PDZ domain also mediates binding to
CC the retromer complex via direct interaction with VPS26 (VPS26A or
CC VPS26B). {ECO:0000250}.
CC -!- DOMAIN: The PX domain mediates binding to phosphatidylinositol 3-
CC phosphate (PtdIns(3P)) and localization to early endosome membranes.
CC {ECO:0000250}.
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; BC142417; AAI42418.1; -; mRNA.
DR RefSeq; NP_001092426.1; NM_001098956.2.
DR AlphaFoldDB; A5PKA5; -.
DR SMR; A5PKA5; -.
DR STRING; 9913.ENSBTAP00000033754; -.
DR PaxDb; A5PKA5; -.
DR PRIDE; A5PKA5; -.
DR Ensembl; ENSBTAT00000081032; ENSBTAP00000057873; ENSBTAG00000001942.
DR GeneID; 513214; -.
DR KEGG; bta:513214; -.
DR CTD; 81609; -.
DR VEuPathDB; HostDB:ENSBTAG00000001942; -.
DR VGNC; VGNC:35105; SNX27.
DR eggNOG; KOG3784; Eukaryota.
DR GeneTree; ENSGT00950000183212; -.
DR HOGENOM; CLU_028138_0_0_1; -.
DR InParanoid; A5PKA5; -.
DR OMA; NCSKDNM; -.
DR OrthoDB; 395943at2759; -.
DR TreeFam; TF318398; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000001942; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; A5PKA5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13338; FERM-like_C_SNX27; 1.
DR CDD; cd01777; FERM_F1_SNX27; 1.
DR CDD; cd06886; PX_SNX27; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR037831; SNX17/27/31.
DR InterPro; IPR028667; SNX27.
DR InterPro; IPR037827; SNX27_FERM-like_dom.
DR InterPro; IPR037833; SNX27_PX.
DR InterPro; IPR037835; SNX27_RA.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12431; PTHR12431; 1.
DR PANTHER; PTHR12431:SF17; PTHR12431:SF17; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50200; RA; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..541
FT /note="Sorting nexin-27"
FT /id="PRO_0000315355"
FT DOMAIN 43..136
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 161..269
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 273..362
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..362
FT /note="FERM-like region F1"
FT /evidence="ECO:0000250"
FT REGION 373..421
FT /note="FERM-like region F2"
FT /evidence="ECO:0000250"
FT REGION 425..525
FT /note="FERM-like region F3"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L92"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L92"
SQ SEQUENCE 541 AA; 61127 MW; 4A7DFBEE886FDE0C CRC64;
MADEDGEGIH PAAPHRNGGG GGGGGSGLHC AGNGGGGGGG PRVVRIVKSE SGYGFNVRGQ
VSEGGQLRSI NGELYAPLQH VSAVLPGGAA DRAGVRKGDR ILEVNGVNVE GATHKQVVDL
IRAGEKELIL TVLSVPPHEA DNLDPSDDSL GQSFYDYTEK QAVPISVPTY KHVEQNGEKF
VVYNVYMAGR QLCSKRYREF AILHQNLKRE FANFTFPRLP GKWPFSLSEQ QLDARRRGLE
EYLEKVCSIR VIGESDIMQE FLSESDENYN GVSDVELRVA LPDGTTVTVR VKKNSTTDQV
YQAIAAKVGM DSTTVNYFAL FEVINHSFVR KLAPNEFPHK LYVQNYTSAV PGTCLTIRKW
LFTTEEEILL NDNDLAVTYF FHQAVDDVKK GYIKAEEKSY QLQKLYEQRK MVMYLNMLRT
CEGYNEIIFP HCACDSRRKG HVITAISITH FKLHACTEEG QLENQVIAFE WDEMQRWDTD
EEGMAFCFEY ARGEKKPRWV KIFTPYFNYM HECFERVFCE LKWRKENIFQ MARSQQRDVA
T
