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Database: UniProt
Entry: A0A0V0RIM1_9BILA
LinkDB: A0A0V0RIM1_9BILA
Original site: A0A0V0RIM1_9BILA 
ID   A0A0V0RIM1_9BILA        Unreviewed;      1385 AA.
AC   A0A0V0RIM1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Zinc transporter 5 {ECO:0000313|EMBL:KRX14272.1};
GN   Name=Slc30a5 {ECO:0000313|EMBL:KRX14272.1};
GN   ORFNames=T07_14725 {ECO:0000313|EMBL:KRX14272.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14272.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX14272.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX14272.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00034634};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|ARBA:ARBA00011182}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000256|ARBA:ARBA00004601}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Sarcoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004369}.
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:KRX14272.1}.
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DR   EMBL; JYDL01000165; KRX14272.1; -; Genomic_DNA.
DR   STRING; 6336.A0A0V0RIM1; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR045316; Msc2-like.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45755; -; 1.
DR   PANTHER; PTHR45755:SF4; ZINC TRANSPORTER 7; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1385
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006867900"
FT   TRANSMEM        817..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        985..1003
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1073..1098
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1118..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1210..1232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1238..1264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..221
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          233..319
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          325..419
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          422..521
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          558..655
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          666..767
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          778..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1385 AA;  154488 MW;  2F13733FB751094B CRC64;
     MLLVSFCQIL VTCAVVLKAP VAGGLVLEPR ARRLVGAEVR PDFNTLSSER HDLRCLLPGR
     SGRFLERKFP SAKYVWYLNG QPIRGSVTNK LQVQMKAEEA ANSPWLKRFY HCAVHLKPEF
     VILSANYSLR QPSLLVEKQN SRRPVIIRPG SIAFVPCPLF RSEPKPVDVY FVVNNTRRLD
     VDNSGRYFVS EIGLQIADVG PQDQGLYQCV VRNARSGQSF RGHPVPVHLS TSPATTQAAL
     LYPPAGVSLV RARFGDNVTL QCVIGSVAAS RIVWVKLNDN LRKLAGVRTR LGNLLLSNVS
     RAHHGSYVCR SGQASASYAL QVQAPLFVRL RLMASRFEDG SWLSDLVCDT HGDRSPTLSW
     FHNGRPLLDA DSITVHWSVQ RRGRNPRWTA TISSPPPPGV YQCVATSGDE STTDSIYVSE
     WPSTTRRRSA TNAHWSKLIR VGPTNTTVKL NSTTFLLCQL HSPGATVSWR HNDTELKLDS
     RRSLVGYGSL QIRQFDYIDQ GWYVCEASDG RWNVTSEAAF VDVEDLTTWS IRRPLMLDNT
     YDATVNNHSG EIPKVPLKLA PPQAVRLDNT SVLLRWELPA KLPDRPWLFR IQLRKMADGY
     DWETLDAEVP GYTNSYVVER LQPSASYRFR YAVIFRNRYQ ETSAKSKRVT MSPEDDGRRI
     ERPYLAPELM TAVSKWPDAI QLKWEQPFGD DAAASPVDGY LVSYRQVYAD KPLRFQNETV
     VGASTREHMI DRLLPATPYE VKLAAYNSAG LSAFSNTLYA STLTLDGKPS SVDFFATDSP
     PPSVVGQSSR KSVSSNKDSS SSNMAPTKPN INSGATILRI AGLTMAAVVV CNVLVGLGIW
     LVKRLVRERA SVRRLRTDRR TFADTSRSIF KETHGRHQPQ NQEQHYSHPA SNATGEEERC
     SGTANGGETA TANESSRIYS THTPASHIRW KRSLAHAVLI TSSHLFWLYG LVLCGPLRSI
     LIYDISSMVV LSALSSLFIG VSGSLKMRGV AFLALGFLFL MFLDRDYNDP ATLMLTTPNA
     PKARTGQFVG YSSAGLPLYV SGEDFLQRTS HSLVAFVKNT IHQILAQPDS RRIFFFLCVN
     LLLSGFVNGL FLVVIAFFIF LEALERLFDP PEVYTERLLF VSVLGLFVNL FGMFVFTGSH
     GHSHGGTTGK HGHSHAGAEV DTAREKKHAN YYDDHHGHAH RHQHGHGHSH GHDRSAANES
     SSLLVHFQRY FYKGVFLHVL ADTLGSVAVI LSTMLIHYFG WLIADPLCSL ILSIIIGLSV
     IPLLRESFDA LLLKTTPTAA EDLNNILKQL IQMDGVISCS RPRCWIVKSD NHVGTLHIQL
     TADSDQQYIT QEAIRLLKSE GINSPIVQVE KDSFFRHMEA LQPSYEPEEP ISTYPRQRNL
     LPMAI
//
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