ID U3KLH0_FICAL Unreviewed; 1892 AA.
AC U3KLH0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=ATPase 13A3 {ECO:0000313|Ensembl:ENSFALP00000015874.2};
GN Name=ATP13A3 {ECO:0000313|Ensembl:ENSFALP00000015874.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000015874.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000015874.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000015874.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR STRING; 59894.ENSFALP00000015874; -.
DR Ensembl; ENSFALT00000015939.2; ENSFALP00000015874.2; ENSFALG00000007219.2.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000155941; -.
DR HOGENOM; CLU_000288_18_18_1; -.
DR Proteomes; UP000016665; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF12; POLYAMINE-TRANSPORTING ATPASE 13A3; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS51450; LRR; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1097..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1127..1146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1843..1867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1670..1722
FT /note="LRRCT"
FT /evidence="ECO:0000259|SMART:SM00082"
SQ SEQUENCE 1892 AA; 213110 MW; 4DF34D8EA5ED1D9B CRC64;
MYEICPHTGS SNRSSISQVE KFHIILNMEK EEKKYVNKAE EDEMEIYGYD LCRWKLVLVA
VGVICSGGFL LLLLYWMPQW RVKATCKRTT LKDCGVVLLR TTDEFKIWFC AKVRIMPSLG
ANPFQNPNPI IHKVSNGHAV HFSESAEENK NESKKYLPIR YFTHHSVKYF WNDSVQSFDV
VRGLDESTFC SAIHNEHSTG LTKGMHDYRK AFYGVNEIAV KVPSIFKLLV KEVLNPFYIF
QLFSVILWIT DEYHYYALAI VIMSVISIVS SLYTIRKQYV MLHDMVAAHS IVRVSVCRGN
QEIEEILSTD LVPGDTMLIP SNGTIMPCDA VLLSGTCIVN ESMLTGESVP VTKINLPNPS
EYPKAVGDEI YSPEVHKRHT LFCGTNVIQT RFYTGELVKA LVVRTGFSTA KGQLVRSILY
PKPTDFKLYR DAYLFLLSLV VVAGVGFLYT IVHSILNEVP ARTIIIESLD IITITVPPAL
PAAMTAGIVY AQRRLKKIGI FCISPQRINI CGQLNLVCFD KTGTLTEDGL DLWGIQRVEN
ACFLLPEETA CSESLLKSEF VACMATCHSL TKIEGVLSGD PLDLKMFEAI GWILEEATEE
ETALHNQIMP TVVRPSKQLS PESKQATDQE MELFELSTGY EIGIVRQFPF SSVLQRMCVI
ARVLGEKRMD AYMKGAPEVI ASLCKQETVP VDFERVLEEY TKQGFRVIAL AHRKLESKLT
WHKVQTISRD AIESNMDFMG LIIMQNKLKQ ETPSVLEDLH KANIRTVMVT GDNMLTAISV
ARDCGMILPQ DKVIIAEALP PKDGQAARIN WHYADTLAKC TSSSPAINSE DIPVKLVHES
LEDLQMTKYH FAMNGKSFAV ILEHFQDLVP KLVLHGTVFA RMAPDQKTQL VEALQNVDYY
VGMCGDGAND CGALKRAHGG ISLSELEASV ASPFTSRTPS ISCVPKLIRE GRAALITSFC
VFKFMALYSI IQYITVTLLY SILSNLGDFQ FLFIDLAIIL VVVFTMSLNP AWTELVARRP
PSGLISGPLL CSVLSQIIIC LAFQALGFFW VKQQSWYEPW TADSDACNGL DAKNTSSAHH
GNETIHDEHY IKNYENTTLF FISSFQYLIV AIVFSKGKPF RQPCYKNFLF VLSVIVLYVF
IFFIMLHPVE PIDEFLELVC VPPEWRLRIV IIVILNAVVS VLTEEAGDRC GVCFLSSLFG
CREKTPKAKY MHLAQELLVD PEWPPKPRTT TEAKVPSSQE NANVSGTSTR MLVFRLSVMI
KLFFQLDASI CPEDCDCSSK NAIYCSGPHI RDLELLNLPC NMTEIHITNA NISYLQDVFA
RMVELQHLIL TSNNIALVSP MAFKGLGRLK VLKLLDNKLV ELPPEAFDDM VQLQQLIIES
NRLKSIEENL FDKLASLQEL YLNKNQLTAL PSDVMKKLTK LRVLNLSRNY LAALPRNIFS
ALTRLERLML YINRLSSIES GMFDSLKELQ ELFLHSNNIH SIAPDAFHCL RKLRTLTLSR
NRLQVLPSGL FLHLHDLSKL TLYRNPLKSL PEVLFGEMRH LGSLWLYHTK LSTIPDFVFS
NLTNLELLVL SFNPELTVLP RNVFSGLNEL RGLSLHTSNI SNLPEGIFLS LQKLQNISLF
DTRLEVLPRN LFQNLKHLQK VYLNSTNLQS LPADFFTALP ELEEVVLDDN PWKCDCQILG
FQEWLQKSMT IVKNVQSLMC HSPMALQNIS LVSLSIDDPE CLPTTAMTQQ TFSSTYSQTL
TSPVMEHFTS SGDSAVTVLS NVETISTPRS VPPATPGFTY SHVEDVGQPG LHFSDVPVQT
SPSIIARTNS VKGTDLTSLV WWDEFPARSS AKPYFITRVT YCQLFLCVHS LILTLQTVVI
VLSLYVMGNT RQLLHSRNFP AQPVVLIRIL RR
//
