ID   A0A0D2U3R4_CAPO3        Unreviewed;       732 AA.
AC   A0A0D2U3R4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Solute carrier family 39, variant 3 {ECO:0000313|EMBL:KJE89851.1};
GN   ORFNames=CAOG_001271 {ECO:0000313|EMBL:KJE89851.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE89851.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|EMBL:KJE89851.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|EMBL:KJE89851.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000256|ARBA:ARBA00006939}.
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DR   EMBL; KE346361; KJE89851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2U3R4; -.
DR   EnsemblProtists; KJE89851; KJE89851; CAOG_001271.
DR   Proteomes; UP000008743; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR003689; ZIP.
DR   PANTHER; PTHR12191; SOLUTE CARRIER FAMILY 39; 1.
DR   PANTHER; PTHR12191:SF30; ZINC TRANSPORTER ZIP4 N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02535; Zip; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        421..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        508..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        666..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          50..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  79445 MW;  F8F7F757A3C5EEE0 CRC64;
     MLGSQVCVHH NISETDVESS TYSTLLLEMF GNGTALSEEN LEHLFLAAGA TQQADHEHEH
     EHEHEHEHEH EDEHEDEHEH EHEDAVAGPC ISVHLLLHAL ELEEESFAGS SLETLATAVI
     YRVATKACVA HDDVETKFVP STQQHFLDAI FDHFGYVGAE NMPVSVMTTI FEKLGLVAGH
     EEDDHEHDHD HEDEHDDHDH DHARRALDEE QPTVRSRRNH EIGHEELTGA LAQAVFDLNG
     VVGRVVFSQD SASHPVDIWA TFSALPNASA AYTLEIRSFR ALANTLPACS AAMLGGLFPD
     ATSGALINTH GALPVGATIN SSYIDSTLSL VDVDFSLVGK SLVLVNTDDD SVVACGNIMD
     TTPRCFTIAQ LLDSFGITET IAQSQLAQLA PGLVSMLVSG ACTNPVTSHA AAASGVTASE
     AWGYGVLATF VVCLVSIIGV LFVPGMKGTR LESNLIYLFF VALAVGVLIG DAIFHLIPQA
     FGVHSHAAGE EEHNHNHEAE EEEHSYDHLW RGCVVIIGIY MMWILEKVLE SSGHGHTHGG
     SAEDSFELNG ATSTKTIELQ EASMKQNSSE KRHIDQIAWL IIISDSIHNF VDGLAMGASF
     YASLSTGLST SIAVLLHEIP HELGDFAILL GAGMTIRQAV FWNLMSSLTC FIGLFVGLGI
     GEDTEARLWI LSLAGGMFLY IALVSLLPQL SKHNTRLNSP QGRKMFLVIN LGILIGLAIM
     LLIGRYEDDI HV
//