ID A0A0V1D8D1_TRIBR Unreviewed; 1724 AA.
AC A0A0V1D8D1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATP-binding cassette sub-family A member 3 {ECO:0000313|EMBL:KRY57756.1};
GN Name=ABCA3 {ECO:0000313|EMBL:KRY57756.1};
GN ORFNames=T03_8357 {ECO:0000313|EMBL:KRY57756.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY57756.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY57756.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY57756.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRY57756.1}.
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DR EMBL; JYDI01000028; KRY57756.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
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:SF250; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 3; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
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; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KRY57756.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1099..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1178..1202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1214..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1247..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1310..1329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 547..779
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1392..1646
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1724 AA; 193877 MW; E08288798FA6A720 CRC64;
MLLQKRSLMW TLLELGIPML FVVILLVLRQ QVDSASRPAV EYADFSITAT VDDFYEPVDG
EPIHSVCFSP VQLYFTPKNN LTIQIMNIVN SRLRLLSKAY ENERTMVEDI MKELNQLDLC
GCSAYGAVVF EEGFLNEAGF GEELKYKIRL SNTPRNSQSR RGTWNIGQAS LFNVGHGWKT
NALYAFPPQN GPRQSNSTDG GKPGYWREGF LILQHAIDKA IIRMLASNVT DVDKFHVHLK
RFVYPPYVDN PFITVIQQHL PVIVLLSFAF SVVYISRTVV MDKELRVKVN NHSYHDSNTL
NRIYACDGLE ILGSFSGAFY LQLPQAGVHL NHVDAFPVHQ HKRQENTGEI GPQRCVVLFL
NLFGYVKVQV RIGFIYSFVF VCHRRFTGNV VAGCTGLIWC SLYWPYFFIQ PRYASVLRST
KLLTCLLVNS AMSYGIQLIG ILEGQNVGLQ WYNLFHRGTM YNNLSMIEVI GMLLVDAVLC
LSIAWYVEAA KPRYNSIRQF ISSKFCHKLF GSRRRKDSIG QVSSESSASN SAVGHFEDCD
NPARVTVSIR KLYKIYENQS SGRKTAVEDL TLDLYYGQIT ALLGHNGAGK STTISILTGV
LAPSCGSVTI NGMDMRKHFD KIQTTLGYCP QYNPLFACMT VYEHLKFYCK LKGRQLMPTE
VDRLLHLLNL ESKRHSLADH LSGGMKRKLC VAIALIGGSE VVLLDEPTTG MDPRARHDAW
QLLLEEKQYR TMLLTTHFME EADLLGDRIA VLSNGTLQCC GTSFFLKRQF GDGYRLKVIF
KYAGKEKAEQ LLKLIEEYIP GAQLSNCIGT EAIYTVPLIK GPKLHALFAS IEQKLDQYDV
ESFGLSIVTM EEVFLRVSPK EPAVDNGQTH LSALADELDH KLETLNRRSR LNKGFKLARQ
QFWALVVKRT LDAVRNGRLL LVQWGVPVLF VAVALAINRC LPDERHSPAL PLTVETYGPT
RIGVYSDARL DGLLANQYRL QFSTEQTVEV VDDGNFTRFV LERIELSDQA LFDRRYVVGA
SFEAGSNGTV HLTGHFNNQP LHAVAVSLNA LDNALLRYAD DHTGEGHWRS LTTVNEPLPA
TEFDRLVNWF EVGVTEFNLA FNLVFGFSLS TGTFVLFSIT ERLSGAKHLQ QLCHVEPALF
WVANFVCDFV VYLFTVFSVL LVFVAFDVDV LIDGWRCLHT LLLFVLYGWA TIPFMYVASF
FFDSATAGYV KMTVFNLLSG NGLLTLVVIT VLLLLNMTDL HETLTWVFMT LFPNFCLGQA
LSTYYFNYFV FSSCEPLMPF CEFTPDAFCC GQDTFTGDQL RWKRPGIGRF LFFLFLHGTL
SVLLLLLWID TRRPRDRDHW SRSVGQLLLG IRRRLFECTR HGGGASQQRL TDRENHDSET
VRTETCCGEP LLRVERLRKE YGSGDRRLVA VDGVSFQVLG GECFGLLGCN GAGKTSTFRM
LSGEQAIDAG DAFVHHTSLR LHWNEAKSMI GYCPQFDALL DNLTVAETLT LFARLHGILA
GDLGDVIDSA ADSVGLSAFK RQRVECLSGG NKRKLSLAIA LINCPPVLLL DEPTSGVDPA
SRRTIWKILE SARRAGVSIV LTSHRYTFAD QIPVQMSYLV VHISNMEECE ALCSRLAIMA
GGEIKCTGSP QQLKSKYGKG YLLIVRVKSE QLIVPFVRML EQSFPGLSVE EIHGTQMHCI
IPFQSSTWSG LFQTLETMIE PCGIVDYMLS QPSLEQIFLT CVSL
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