ID A0A1S3G7I7_DIPOR Unreviewed; 2840 AA.
AC A0A1S3G7I7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-binding cassette sub-family A member 2 {ECO:0000313|RefSeq:XP_012884798.1};
GN Name=Abca2 {ECO:0000313|RefSeq:XP_012884798.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012884798.1};
RN [1] {ECO:0000313|RefSeq:XP_012884798.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012884798.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_012884798.1; XM_013029344.1.
DR STRING; 10020.ENSDORP00000016009; -.
DR GeneID; 105995578; -.
DR KEGG; dord:105995578; -.
DR CTD; 20; -.
DR InParanoid; A0A1S3G7I7; -.
DR OrthoDB; 6951at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF225; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 2; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840,
KW ECO:0000313|RefSeq:XP_012884798.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1110..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1153..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1294..1317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2197..2220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2250..2271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2277..2296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2308..2333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1394..1625
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 2455..2690
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1990..2033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2840 AA; 313091 MW; 967F1016358BC46E CRC64;
MWPLPSPGGT RPQHSQVGSG EALPPHRWPH VDRPFQWVLA FEIFIPLVLF FILLGLRQKK
PTISVKEVSF YTAAPLTSAG ILPVMQSLCP DGQRDEFGFL QYANSTVTQL LERLNRVVEE
GNLFDPARPN LGLELEALRQ HLEALSSDPG TWGSPPDRSA VASFSLDSVA RDPRELGRFL
MQNLSLPNGT AQALLAARVD PSEVYRLLFG PLPVLDGESY FLRGREPWSH PGSEPLFRME
ELLLAPARLE RLTCALGSGG LDRILAMPEG RQTALQGYRD VVCSGQAGTR AQRFTELAAV
LRNQLDVAKI AQQLGLDAPN SSDSQPRAPS PRGLQALLGD LLDAQKVLQD VDVLSALALL
LPQGACTGRT PAPPASSRGG VANGTGPGPG TGSNITAEDS TQAAAAPVTP DTLQGQCSAF
VQLWAGLQPI LCGNNRGLTH ALSASVSLPI LDRSPCPAFY TAAPLTSAGI LPVMQSLCPD
GQRDEFGFLQ YANSTVTQLL ERLNRVVEEG NLFDPARPNL GLELEALRQH LEALSSDPGT
WGSPPDRSAV ASFSLDSVAR DPRELGRFLM QNLSLPNGTA QALLAARVDP SEVYRLLFGP
LPVLDGESYF LRGREPWSHP GSEPLFRMEE LLLAPARLER LTCALGSGGL DRILAMPEGR
QTALQGYRDV VCSGQAGTRA QRFTELAAVL RNQLDVAKIA QQLGLDAPNS SDSQPRAPSP
RGLQALLGDL LDAQKVLQDV DVLSALALLL PQGACTGRTP APPASSRGGV ANGTGPGPGT
GSNITAEDST QAAAAPVTPD TLQGQCSAFV QLWAGLQPIL CGNNRTIEPE ALRRGNMSSL
GFTSKEQRNL GLLVHLMTSN PKILYAPAGS EADRVILKAN ETFAFVGNVT HYAQVWLNIS
AEIRSFLEQG RLQQHLHWLQ QYVTELQLHP EALNLSLDEL PPALRQGNFS LPNGTALLQQ
LDTIDNAACG WVQFMSKVSV DIFKGFPDEE SIVNYTLNQA YQDNVTVFAS VIFQTRKDGS
LPPHVHYKIR QNSSFTEKTN EIRRAYWRPG PNTGGRFYFL YGFVWIQDMM ERAIINTFVG
HDVVEPGNYV QMFPYPCYTR DDFLFVIEHM MPLCMVISWV YSVAMTIQHI VAEKEHRLKE
VMKTMGLNNA VHWVAWFITG FVQLSISVTA LTAILKYGQV LMHSHVAIIW LFLAVYAVAT
IMFCFLVSVL YSKAKLASAC GGIIYFLSYV PYMYVAIREE VAHDKITAFE KCIASLMSTT
AFGLGSKYFA LYEVAGVGIQ WHTFSQSPVE GDDFNLLLAV TMLMVDAVVY GVLTWYIEAV
HPGMYGLPRP WYFPLQKSYW LGSGRTETWE WSWPWVRAPR LSVMEEDQAC AMESRRFEEM
RGMEEEPTHL PLVVCVDRLT KVYKNDKKLA LNKLSLNLYE NQVVSFLGHN GAGKTTTMSI
LTGLFPPTSG SATIYGHDIR TEMDAIRKNL GMCPQHNVLF DRLTVEEHLW FYSRLKSMAQ
EEVHKEMDKM IEDLELSNKR HSLVQTLSGG MKRKLSVAIA FVGGSRAIIL DEPTAGVDPY
ARRAIWDLIL KYKPGRTILL STHHMDEAEL LGDRIAIVSH GKLRCCGSPL FLKGAYGDGY
RLTLVKRPAE PGAPQEPGLA SSPPGRAQLS SCSEPQVSQF IRKHVASCLL VSDTSTELSY
ILPSEAAKKG AFERLFQHLE HSLDALHLSS FGLMDTTLEE VFLKVSEEDQ SLENSEADVK
ESRKDVLPGA EGPVCGEDQA GNLARCSELA QSQASLQSAS SVGSARGDEG AGYADVYGDY
RPLFDNLQDP DNVSLQEAEA EVLTRVGQGS HKLEGWWLKV RQFHGLLVKR FHCARRNSKA
LCSQILLPAF FVCVAMTVAL SVPEIGDLPP LVLSPSQYHN YTQPRGNFIP YANEERREYR
LRLSPDASPQ QLVSTFRLPS GVGATCVLKS PANGSLGPTV NLSSGESRLL AARFFDGMCL
ESFTQGLPLS NFVPPPPSPA PSDSPMSSDE DLPQAWNASL PPTTGPETWT SAPSLPRLVR
EPVRCTCSAQ GTGFSCPSSV GGHPPQMRVV TGDILMDITG HNVSEYLLFT SDRFRLHRYG
ALTFGNVLKS IPASFGTRAP PMVRKIAVRR AAQVLYNNKG YHSMPTYLNS LNNAILRANL
PKGKGNPAAY GITVTNHPMN KTSASLSLDY LLQGTDVVIA IFIIVAMSFV PASFVVFLVA
EKSTKAKHLQ FVSGCNPVTY WLANYVWDML NYLVPATCCV IILFVFDLPA YTSPTNFPAV
LSLFLLYGWS ITPIMYPASF WFEVPSSAYV FLIVINLFIG ITATVATFLL QLFEHDKDLK
AVNSYLKSCF LIFPNYNLGH GLMEMAYNEY INEYYAKIGQ FDKMKSPFEW DIVTRGLVAM
TVEGVVGFLL TIMCQYNFLR QPPRMPVSTK PVEDDVDVAA ERQRVLRGDA DNDMVKIENL
TKVYKSRKIG RILAVDRLCL GVRPGECFGL LGVNGAGKTS TFKMLTGDES TTGGEAFVNG
HSVLKELPQV QQSLGYCPQF DALFDELTAR EHLQLYTRLR GIPWKDEARV VKWALEKLEL
TKYADKPAGT YSGGNKRKLS TAIALIGYPA FIFLDEPTTG MDPKARRFLW NLILDLIKTG
RSVVLTSHSM EECEALCTRL AIMVNGRLRC LGSIQHLKNR FGDGYMITVR TKCSQNVKDV
VCFFNRNFPE AVLKERHHTK VQYQLKSEHV SLAQVFSKME QVVGVLGIED YSVSQTTLDN
VFVNFAKKQS DNLEQQETEP PSALRSPLGR LLSLLRPRPA PTELRALVTD EPEDLDTEDE
GLISFEEERV QLSFNTDTLC
//
