ID A0A091G9K4_9AVES Unreviewed; 946 AA.
AC A0A091G9K4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE SubName: Full=Sorting nexin-14 {ECO:0000313|EMBL:KFO79055.1};
GN ORFNames=N303_02346 {ECO:0000313|EMBL:KFO79055.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO79055.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO79055.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO79055.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KL447974; KFO79055.1; -; Genomic_DNA.
DR RefSeq; XP_009563081.1; XM_009564786.1.
DR AlphaFoldDB; A0A091G9K4; -.
DR STRING; 55661.A0A091G9K4; -.
DR GeneID; 104062689; -.
DR KEGG; cuca:104062689; -.
DR CTD; 57231; -.
DR OrthoDB; 2877434at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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:UP000053760};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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 570..690
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
SQ SEQUENCE 946 AA; 109696 MW; F2DA53AE845F2A60 CRC64;
MGGARAAARR LRQRVRGAGA VREVCRQYPL SCCLLLGLGA ATLLLNRYLH VLMIFWSFVA
GVITFYCSLG PDSLLPSILF TIKYKPKQLE LPELFPHGHS CAVCGKVKCK RHRPTLLLEN
YQPWLDLKVP SKVDASLSEV LELVLENFIY PWYRNITDDE SSVDELRGTL RFFASVLVRR
IHKVDIPTVV TKKMLKAAMK HIEVIAKARQ KVKNAEFLQQ AALEEYGPEL HVALRSRRDE
LHYLRKLTEL LFPYILPPKS TECRSLALLI REILPGSVFL PSMDFLADPD TVNHLLLIFI
DDSPPEKATE PTSSLVPFLQ KFAEPRNKKP SVLKLELKEI RDQQDLLFRF MNFLKQEGAV
HVLQFCLTVE EFNDRILRPE LSDTEKMSLH EEVQKIYKTY CLDESIDKIR FDPFIVEEIQ
RIAEGPYMDV VKLQTMRCLF EAYEHVLSLL ENVFTPMFCH SDEYFRHLLR GAESPTRNSK
FNRSSLSLDD FRTTQKRGES FGISRIGNKI KGVFKSSAME GAMLPNYNLN EGEDDFIEEG
VMVMEDDSPE EAVSTPNTPR NLAAWKISIP YVDFFDDPSL ERKDRKERIP VFCIDVERND
RRAVGHEPEH WSVYRRYLEF YVLESKLTEF HGTFPDAQLP SKRIIGPKNY EFLKSKREEF
QEYLQKLLQH PELSNSQLLA DFLSPNGGET QFLDKMLPDV NLGKIIKSVP GKLMKEKGQH
LEPFIMNFIN SCESPKPKPC RPELTILSPT SENNKKLFND LFKNNANRSE NTERRQNQNY
FMEVMTVEGV YDYLMYVGRV VFRIPDWLHH LLMGGRILFK NTLELYTDYY LHCKLEQLFQ
EHRLVSLITL LRDAVFCENT EPRSLQDKQK RAKQTFEEMM RYIPDLIGKC IGEEAKYEGI
RLLFDGMQQP VLNKQLTYVL LDIGIQELFP ELSKGPKEVS SASGWM
//