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Database: UniProt
Entry: A0A0L0BLG1_LUCCU
LinkDB: A0A0L0BLG1_LUCCU
Original site: A0A0L0BLG1_LUCCU 
ID   A0A0L0BLG1_LUCCU        Unreviewed;       922 AA.
AC   A0A0L0BLG1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Calcium-binding mitochondrial carrier protein Aralar1 {ECO:0000313|EMBL:KNC20798.1};
GN   ORFNames=FF38_00106 {ECO:0000313|EMBL:KNC20798.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC20798.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC20798.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC20798.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC20798.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000256|ARBA:ARBA00038674}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375}.
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:KNC20798.1}.
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DR   EMBL; JRES01001702; KNC20798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BLG1; -.
DR   STRING; 7375.A0A0L0BLG1; -.
DR   EnsemblMetazoa; KNC20798; KNC20798; FF38_00106.
DR   OMA; HYIWIST; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0043490; P:malate-aspartate shuttle; IEA:UniProt.
DR   CDD; cd00037; CLECT; 1.
DR   CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45678:SF9; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN ARALAR1; 1.
DR   PANTHER; PTHR45678; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER 1-RELATED; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          21..128
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          335..370
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          406..441
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          570..661
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          669..753
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          761..849
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   COILED          140..214
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   922 AA;  103985 MW;  0E24AE2CD910AEC0 CRC64;
     MFNNFQPIVW IIKPVQCQDY TWFDALTKCA SMNMSLATID TKEKSDEITD LLSKTFGNVN
     GMWIGAIANG KDHHYIWIST GNEITFSNWS PGEPNFQNAQ EYCVLTGWTD KIKWNDGGCY
     SLQGVICDFN DYNYNLNELK EFYEAKLQEE MLKEQELQNQ LQNELAKEQE LKDQLQKELE
     NKNQNQLENE QELQKQLKQE LEKEQKLQSQ LQKNQLLLQM LLDYRFYNDD RNNINVTNYL
     KTKKDYQLQI IAGHSFLKRA STDKLREVFQ KYATYEKNGE HFMTSEDFVR KFLGLFTDAA
     FNDESVRLLA GIADTSKDGL ISFSEFQAFE GLLCTPDALY KTAFQLFDRQ GNGTVSYSDF
     ADVVQKTELH SKIPFSLDSP FIKRYFGEKK QRLINYAEFT QLLHDFHEEY AMEAFRSKDP
     AGSGYISPLD FQDIMVKVKK HLLTADVKDN LVAVTEGHKV SFPYFMAFTS LLNNMELIKR
     IYLHSTQGNR TEPVTKDELL YAAQTMSQIT PLEIDILFQL TGALHQTGRI VYSDLSNIAP
     EHYTKHITTR LAEIKAVESP ADRSAFIQIL ESTYRFTLGS LAGAVGATVV YPIDLVKTRM
     QNQRTGSYIG EVAYRNSWDC FKKVIRHEGV MGLYRGLLPQ LMGVAPEKAI KLTVNDLVRD
     KCTDKQGQIP LWSEILAGGC AGASQVVFTN PLEIVKIRLQ VAGEIAGGSK VRALSVVRDL
     GLFGLYKGAR ACLLRDVPFS AIYFPTYAHT KALFADEDGY NHPLTLLAAG AIAGVPAASL
     VTPADVIKTR LQVVARSGQT TYSGVWDATK KIMAEEGPRA FWKGTAARVF RSSPQFGVTL
     VTYELLQRLF YVDFGGSHPT GSEVNKLKAI DTSNVRINAD HIGGYRAAVP LLNGIESKFG
     LFLPRFGHAQ PQSSATTAKT TS
//
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