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Database: UniProt
Entry: A0A0Q3UQ01_AMAAE
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ID   A0A0Q3UQ01_AMAAE        Unreviewed;       835 AA.
AC   A0A0Q3UQ01;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit gamma {ECO:0000256|ARBA:ARBA00034844};
DE   AltName: Full=FXYD domain-containing ion transport regulator 2 {ECO:0000256|ARBA:ARBA00034896};
DE   AltName: Full=Sodium pump gamma chain {ECO:0000256|ARBA:ARBA00034918};
GN   ORFNames=AAES_155156 {ECO:0000313|EMBL:KQK74522.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74522.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK74522.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74522.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in forming the receptor site for cardiac
CC       glycoside binding or may modulate the transport function of the sodium
CC       ATPase. {ECO:0000256|ARBA:ARBA00034654}.
CC   -!- SUBUNIT: Regulatory subunit of the sodium/potassium-transporting ATPase
CC       which is composed of a catalytic alpha subunit, an auxiliary non-
CC       catalytic beta subunit and an additional regulatory subunit.
CC       {ECO:0000256|ARBA:ARBA00034793}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004183}; Single-
CC       pass type III membrane protein {ECO:0000256|ARBA:ARBA00004183}.
CC   -!- SIMILARITY: Belongs to the FXYD family.
CC       {ECO:0000256|ARBA:ARBA00005948}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK74522.1}.
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DR   EMBL; LMAW01003036; KQK74522.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3UQ01; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0043269; P:regulation of monoatomic ion transport; IEA:InterPro.
DR   CDD; cd20318; FXYD2; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.20.5.780; Single helix bin; 2.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR047282; ATNG.
DR   InterPro; IPR047297; FXYD_motif.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF14; TRANSMEMBRANE PROTEASE SERINE 3-LIKE; 1.
DR   Pfam; PF02038; ATP1G1_PLM_MAT8; 2.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01310; FXYD; 2.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:KQK74522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        563..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        630..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          146..228
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          238..471
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  92260 MW;  1C99C0937446D3E6 CRC64;
     MDLKPSLTTA SPSSAPPSLH ASAARNIFGS RPPRPRENVL CTSFKPYSPE SSPALAPCTA
     CESTRSSMFR APCMSQRRLV LIFCVSILIA LLIALILLFM FWRSQTGIVY KEPAESCKDN
     PVRCNGIVDC SQRSDELGCV RFASDESLLQ VYSSAESQWL PVCSNAWDES FSRKTCQQLG
     FQNASQTEYV PLHISGKSLT VTSEHETIQQ SLNSSQCLTG KYVSLRCTTC GQRISGRIIG
     GKETSVSKWP WQVSVQYGPV HICGGTIIDA QWVLTAAHCF FMNSMKILND WRVYGGVSDL
     KQQAEAIPVS QVIINSNYSD DHDDYDIALM KLSRPLTLSA QVRPACLPMY GQRFQTGRSC
     FITGFGKTRE NEDNTSPKLR EAEVKLIDYK ICNSDKVYEG YLTPRMMCAG YLQGGKDACQ
     GDSGGPLVCE DNGRWYVAGV TSWGTGCGQK NKPGVYTRVT KLLNWIYSKM EDLLLPDLLW
     LSPQGSGFLQ LDLGESMQVL SSPEAKPGST TTEPALAARC PAAAMEAVLI FLCSLLVPAA
     VADVATQEKX EDPFNYDYQS LRIGGLVFAV VLFTVGILLI LSRRCRCSFN QKPRAPGDEE
     AQAENLITSN EQAPEQGLDR FSYDYETIRN GGLIFAIVAF VVGLLIILTH TEDVGTSLYF
     VNDSIQQVTF SSTVGVVIPC PAAGSPSAXL RWYLATGDDI YDVPHIRHVH VNGTLQLYPF
     SPSAFNSFIH DNDYFCTAEN SAGKIRSPNI RVKAVFREPY TVRVEDQRSM RGNVAVFKCL
     IPSSVQEYVS VVSWEKDTVS IIPGELPQET LWRQQPWYPL SKTFSSDSGR RIAMI
//
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