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Database: UniProt
Entry: A0A151NTM5_ALLMI
LinkDB: A0A151NTM5_ALLMI
Original site: A0A151NTM5_ALLMI 
ID   A0A151NTM5_ALLMI        Unreviewed;      2167 AA.
AC   A0A151NTM5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative cation-transporting ATPase 13A2 isoform B {ECO:0000313|EMBL:KYO40010.1};
GN   Name=ATP13A2 {ECO:0000313|EMBL:KYO40010.1};
GN   ORFNames=Y1Q_0012966 {ECO:0000313|EMBL:KYO40010.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40010.1};
RN   [1] {ECO:0000313|EMBL:KYO40010.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40010.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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}.
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:KYO40010.1}.
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DR   EMBL; AKHW03002106; KYO40010.1; -; Genomic_DNA.
DR   STRING; 8496.A0A151NTM5; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006544; P-type_TPase_V.
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; 2.
DR   NCBIfam; TIGR01657; P-ATPase-V; 2.
DR   PANTHER; PTHR45630:SF4; CATION-TRANSPORTING ATPASE 13A5-RELATED; 1.
DR   PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR   Pfam; PF13246; Cation_ATPase; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 2.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 2.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 3.
DR   SUPFAM; SSF56784; HAD-like; 2.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
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        53..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        894..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        918..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        958..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1034..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1064..1084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1104..1121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1245..1262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1268..1287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1444..1465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1882..1904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1950..1972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2015..2032
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2044..2064
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2084..2105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..250
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2167 AA;  239708 MW;  87E175938A17E2C4 CRC64;
     MPSMEPRQGV PGERSSCQPR GQKGGCRLRK QSVKLHNLVE EHNRVQQSAS DTITMALLLL
     TVPVPPAIPA ALTTAIVYAQ RRLKQKQIFC ISPQRINICG QINLVCFEKD EFHLYSRKVV
     TWISVSALPS FKPGHPLVAD ESSVINEALM KPDLKVRCIQ VQKIRYLWNI SGKRFQKIGC
     LEDHHTCSDM HDKFGSGLSH EDQAIRRLIC GPNTIDVRVV PIWKLLVKEV LHPFYVFQLF
     SICLWFADDY MEYASAILLM SLLSVSLTVY DLRKQSVKLH RLVESHTNVT VTVFRKMEGC
     QKVKSHQLVP GDTLVLTEGK SFLPCDAVLI SGRCIVNESM LTGESIPVTK APLPYANNAE
     PWKTHCSEEY KRHILFCGTE VIQTKADGEG LVKAIVLQTG FNTAKGDLVR SILYPKPINF
     KLYRDAMSFL MCLIALATAG MIYTVCIFAL NGEEPGDIVK KALDIITIAV PPALPAALTT
     GIIYTQRRLK NKGIFCISPQ RINMCGQLNL FCFDKTGTLT EDGLDLLGVV PAEGNRFQEV
     HSFASGQTLP WGPVCGAMVS CHSLVLLEGR TQGDPLDLKM FEATGWELEE SGGDHAAGGG
     SVHTTMIKPG PKAGQVPVRG MAILHHFPFT SALRRMSVIA QEIGGAQHVF MKGAPETVAE
     FCRPETVPSQ LTSELQLYTA QGFRVIGLAH RVLQAGNQTA RLIRKDVESG LVFLGLLIME
     NRLKRETKPV LEELSAACIR NVMVTGDNIQ TAVTVAKNAS MISPTSQVIL VEAKELPGTP
     AASVTWTLME GSHLNGSKGL LLLNGTVFAR MSPGQKSSLV EEFQKLGYYV GMCGDGANDC
     GALKVAHAGI SLSEEEASVA SPFTTRTPTI ECVPQLIREG RAALVTSLCM FKYMALYSII
     QYLGVLLLYW QLNSFGNYQF LFQDLAINTV IGVTMSLNGA YPKLVPYRPP SQLVSPPLLL
     SLVLHILFSL GLQICGFLVV QEQPWYSKED ISSACLSGKT SLANHSSSSS SLNGMGNATL
     GQEVDNGFKS YENSTVWLLS TINCIAVALV VSKGKPFRQP AYTNYQFVLA LTVQLGVCIF
     LMFADMEGVY SIFDLVCTPP VWRVSMLIML AITFAASLLV EDEFQRYTRK KVTWTDLSTL
     TVSVSDKPDG LLIADKDSII NRAIMKPELK VRCIQVQKIR YIWDISAKQF HKVGSLEDSN
     SCNDMHQKFG AGLTREEQNI RRLVCGPNAI EIEIRPIWKL LFKEILNPFY VFQAFTLTLW
     ITQGYVEYSV AIIILSIISI SLTVFDLRQQ SVKLHNLVEE HNRVQVKACT KDEGCKTLES
     HLLVPGDVLV LEGKKLSLPC DAVLIDGGCI VNEGMLTGES IPVTKTALPH ADNTMPWKTH
     SVEDYRRHVL FCGTEVIQTK PSGRGPVRAV VLQTGFNTAK GDLVRSILYP KPVNFKLYRD
     AFKFIVGLAV IGVLGLIYTV CVYAYRKTGT LTEDGLDLWG VIPSEGSRFQ NVHSFTSGAP
     LPWGPVCGAM ASCHSLALLD GKIQGDPLDL KMFEGTNWEM EDPSDTEGLD SCIVIKPGPN
     ASNAPVEGIV ILHQFPFSSA LQRMAVVTQE VGKNQYDLYM KGAPEMVASF CRPETVPTDF
     VKELQVYTTQ GFRVIALAHK ALNVGKDVAV DSLEREDVES GLAFLGLLIM ENRLKRETKP
     VLEELSAARI RSVMVTGDNL QTAVTVAKNS EMIPKSSPVI LIEANEPEGT TPASITWQLM
     EESKQATAET NEVYVDIETR TPPDRDVHSH HFAMNGKSYQ VIVKHFSSLL PKILVNGTVF
     ARMSPNQKSS LVEEFQNLNY YVGMCGDGAN DCGALKAAHA GISLSEQEAS VASPFTSQIP
     NIECVPELIR EGRAALVASF AVFKYLTLYG LIQFIGTSLL FWQLQIFGNY QYLIEDVGIT
     LLVCLTMSLT HAYPKLAPYR PPGQLISPPL LLSIVLNVCF TTTILFGGFL LVKQQPWYSE
     TPNPRGCPQP LAPVSTATTN ATHVSSSVLS YEGTTMWPLA TINCIIIAFV FSKGKPFRKP
     IYTNYIFSLF LLLQLGICIF ILFADIDAVY RGMELLCTPT MWRVYILITA LVTFCVSFVV
     EDLVLQNRRL WLLIKKCFGF RSKSQYRKWQ RKLATDPTWP PLQRTDFAEN GKNEIYTNPA
     YEHSEEK
//
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