ID A0A452F1Y3_CAPHI Unreviewed; 937 AA.
AC A0A452F1Y3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Sorting nexin 14 {ECO:0000313|Ensembl:ENSCHIP00000018337.1};
GN Name=SNX14 {ECO:0000313|Ensembl:ENSCHIP00000018337.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018337.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018337.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018337.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; LWLT01000012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017908666.1; XM_018053177.1.
DR AlphaFoldDB; A0A452F1Y3; -.
DR Ensembl; ENSCHIT00000026153.1; ENSCHIP00000018337.1; ENSCHIG00000017765.1.
DR GeneID; 102183328; -.
DR CTD; 57231; -.
DR GeneTree; ENSGT00950000182856; -.
DR OrthoDB; 2877434at2759; -.
DR Proteomes; UP000291000; Chromosome 9.
DR Bgee; ENSCHIG00000017765; Expressed in frontal cortex and 18 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:InterPro.
DR CDD; cd06877; PX_SNX14; 1.
DR CDD; cd08722; RGS_SNX14; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR037436; SNX14_PX.
DR InterPro; IPR037892; SNX14_RGS.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR PANTHER; PTHR22775:SF44; SORTING NEXIN-14; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..304
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 336..468
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 561..681
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
SQ SEQUENCE 937 AA; 109197 MW; 0D60673A4C8C993E CRC64;
MAPWVRTMGE KLKQRLRLDV GREICRQYPL FCFLLLCLSA ASLLLNRYLH VLMIFWSFVA
GVVTFYCSLG PDSLLPNIFF MIKYKPKQLG LQELFPQGRS CAVCGKVKCK RHRPSLLLEN
YQPWLDLKIS SKVDASLSEV LELVLENFVY PWYRDVTDDE SFVDELRIIL RFFASVLIRR
IHKVDIPSII TKKLLKAAMK HIEVIVKASQ KVENTEFLQQ AALEEYGPEL HVALRSRRDE
LHYLRKLTEL LFPYILPPKA TDCRSLTLLL REILSGSVFL PSLDFLADPD TVNHLLIIFI
DDSPPEKATE PPSPLVPFLQ KFAEPRNKKP SVLKLELKQI REQQDLLFRF MNFLKQEGAV
HVLQICLTVE EFNDRILRPE LSNDEMLSLH EELQKIYKTY CLDESVDKIR FDPFIVEEIQ
KIAEGPYIDV VKLQTMRCLF EAYEHVLSLL ENVFTPMFCH SDEYFRQLLR GAESPTRNSK
FNRSTQKRGE SFGISRIGSK IKGVFKSTTM EGAMLPNYGL AEGEDDFIEE GIVVMEDDSP
VEAVNTPNTP RNLAAWKISI PYVDFFEDTS SERREKKERI PVFCIDVERN DRRAVGHEPE
HWSVYRRYLE FYVLESKLTE FHGTFPDAQL PSKRIIGPKN YEFLKSKREE FQEYLQKLLQ
HPELSNSQLL ADFLSPNGGE TQFLDKILPD VNLGKIIKSV PGKLMKEKGQ HLEPFIMNFI
NSCESPKPKP SKPELTILSP TSENNKKLFN DLYKNNANRA ENTERRQNQN YFMEMMTVEG
VYDYLMYVGQ VVFQVPDWLH HLLMGTRILF KNTLEMYTDY YLHCKLEQLF QEHRLVSLIT
LLRDAVFCEN TEPRSLQDKQ KRAKQTFEGM MNYIPDLIVK CIGEEAKYES IRLLFDGLQQ
PVLNKQLTYV LLDIVIQELF PELNKVQKEV TSVTSWI
//