ID L5KVE5_PTEAL Unreviewed; 727 AA.
AC L5KVE5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Metal transporter {ECO:0000256|RuleBase:RU369091};
GN ORFNames=PAL_GLEAN10005588 {ECO:0000313|EMBL:ELK14798.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14798.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Metal transporter. {ECO:0000256|RuleBase:RU369091}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU369091};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU369091}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000256|ARBA:ARBA00010484,
CC ECO:0000256|RuleBase:RU369091}.
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DR EMBL; KB030557; ELK14798.1; -; Genomic_DNA.
DR RefSeq; XP_006909488.1; XM_006909426.1.
DR AlphaFoldDB; L5KVE5; -.
DR STRING; 9402.L5KVE5; -.
DR eggNOG; KOG2118; Eukaryota.
DR InParanoid; L5KVE5; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; METAL TRANSPORTER CNNM; 1.
DR PANTHER; PTHR12064:SF26; METAL TRANSPORTER CNNM4; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; CNNM; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 134..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369091"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369091"
FT TRANSMEM 219..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369091"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369091"
FT DOMAIN 130..310
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 397..463
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 599..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 81705 MW; 06260ACDDFB54C1A CRC64;
MRLASCNKSC GMNPDGIIFV SEGSTVNLRL YGHGLGSISS NLISFTEVDN SEALHNSTHC
PELTKDLVVQ QLVNVSRGDT SGVLVVLTKF LRRSENMKLY ALCTRAGADG PWRRWTDKDS
LLFMMEEEGR FLPLWLHILL ILVLLVLSGI FSGLNLGLMA LDPMELRIVQ NCGTEKERRY
ARKIEPIRRK GNYLLCSLLL GNVLVNTSLT ILLDNLIGSG LMAVASSTIG IVIFGEIVPQ
ALCSRHGLAV GANTIVLTKF FMLLTFPLSF PISKLLDFFL GQEIRTVYNR EKLMEMLKVT
EPYNDLVKEE LNMIQGALEL RTKTVEDIMT QLHDCFMIRS DAILDFSTMS EIMESGYTRI
PVFEDEQSNI VDILYVKDLA FVDPDDCTPL KTITRFYNHP VHFVFHDTKL DAMLEEFKKG
KSHLAIVQKV NNEGEGDPFY EVLGLVTLED VIEEIIKSEI LDESDMYTDN RSRKRVSEKN
KRDFSAFKDA DNELKVKISP QLLLAAHRFL ATEVPQFSPS LVSEKILLRL LKYPDVIQEL
RFDEHNKHCA RHFLYSRNKP ADYFVLILQG KVEVEAGKEN MKFETGAFSY YGTMALSLSP
SDRSPSHPSP LSRSASLSYP ERTDLTSTAP LASSSNQLGG SALGQYVSDF SVRALTDLQY
IKITRQQYQN GLLASRMENC PQFALDGCTV CTESRAEKPE LPVVDETTAL LNEHNAMLHR
ASPESAI
//
