ID   S39AB_HUMAN             Reviewed;         342 AA.
AC   Q8N1S5; B2R8H7; Q8WZ81;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Zinc transporter ZIP11;
DE   AltName: Full=Solute carrier family 39 member 11;
DE   AltName: Full=Zrt- and Irt-like protein 11;
DE            Short=ZIP-11;
GN   Name=SLC39A11; Synonyms=C17orf26, ZIP11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-111.
RX   PubMed=11707075; DOI=10.1006/geno.2001.6648;
RA   Bagheri-Fam S., Ferraz C., Demaille J., Scherer G., Pfeifer D.;
RT   "Comparative genomics of the SOX9 region in human and Fugu rubripes:
RT   conservation of short regulatory sequence elements within large intergenic
RT   regions.";
RL   Genomics 78:73-82(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ALA-111.
RC   TISSUE=Kidney, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-111.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-111.
RC   TISSUE=Blood;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Zinc importer that regulates cytosolic zinc concentrations
CC       either via zinc influx from the extracellular compartment or efflux
CC       from intracellular organelles such as Golgi apparatus. May transport
CC       copper ions as well. The transport mechanism remains to be elucidated.
CC       {ECO:0000250|UniProtKB:Q8BWY7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8BWY7};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29353;
CC         Evidence={ECO:0000250|UniProtKB:Q8BWY7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cu(2+)(in) = Cu(2+)(out); Xref=Rhea:RHEA:28703,
CC         ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q8BWY7};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28705;
CC         Evidence={ECO:0000250|UniProtKB:Q8BWY7};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BWY7};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8BWY7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8BWY7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8BWY7}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q8BWY7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N1S5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N1S5-2; Sequence=VSP_028976;
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000305}.
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DR   EMBL; AF331643; AAL32175.1; -; mRNA.
DR   EMBL; AK095227; BAC04504.1; -; mRNA.
DR   EMBL; AK313376; BAG36174.1; -; mRNA.
DR   EMBL; AC011120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC080037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89107.1; -; Genomic_DNA.
DR   EMBL; BC035631; AAH35631.1; -; mRNA.
DR   CCDS; CCDS11690.1; -. [Q8N1S5-2]
DR   CCDS; CCDS54160.1; -. [Q8N1S5-1]
DR   RefSeq; NP_001153242.1; NM_001159770.1. [Q8N1S5-1]
DR   RefSeq; NP_631916.2; NM_139177.3. [Q8N1S5-2]
DR   RefSeq; XP_005257191.1; XM_005257134.3.
DR   RefSeq; XP_006721817.1; XM_006721754.3.
DR   RefSeq; XP_006721818.1; XM_006721755.2. [Q8N1S5-1]
DR   RefSeq; XP_011522795.1; XM_011524493.1. [Q8N1S5-1]
DR   RefSeq; XP_011522796.1; XM_011524494.2. [Q8N1S5-1]
DR   RefSeq; XP_016879819.1; XM_017024330.1. [Q8N1S5-2]
DR   RefSeq; XP_016879820.1; XM_017024331.1.
DR   RefSeq; XP_016879821.1; XM_017024332.1. [Q8N1S5-2]
DR   AlphaFoldDB; Q8N1S5; -.
DR   SMR; Q8N1S5; -.
DR   BioGRID; 128379; 74.
DR   IntAct; Q8N1S5; 25.
DR   STRING; 9606.ENSP00000445829; -.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   TCDB; 2.A.5.5.2; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR   iPTMnet; Q8N1S5; -.
DR   PhosphoSitePlus; Q8N1S5; -.
DR   BioMuta; SLC39A11; -.
DR   DMDM; 313104189; -.
DR   EPD; Q8N1S5; -.
DR   jPOST; Q8N1S5; -.
DR   MassIVE; Q8N1S5; -.
DR   MaxQB; Q8N1S5; -.
DR   PaxDb; 9606-ENSP00000445829; -.
DR   PeptideAtlas; Q8N1S5; -.
DR   ProteomicsDB; 71629; -. [Q8N1S5-1]
DR   ProteomicsDB; 71630; -. [Q8N1S5-2]
DR   Pumba; Q8N1S5; -.
DR   Antibodypedia; 31896; 140 antibodies from 26 providers.
DR   DNASU; 201266; -.
DR   Ensembl; ENST00000255559.8; ENSP00000255559.3; ENSG00000133195.12. [Q8N1S5-2]
DR   Ensembl; ENST00000542342.6; ENSP00000445829.2; ENSG00000133195.12. [Q8N1S5-1]
DR   GeneID; 201266; -.
DR   KEGG; hsa:201266; -.
DR   MANE-Select; ENST00000255559.8; ENSP00000255559.3; NM_139177.4; NP_631916.2. [Q8N1S5-2]
DR   UCSC; uc002jja.4; human. [Q8N1S5-1]
DR   AGR; HGNC:14463; -.
DR   CTD; 201266; -.
DR   DisGeNET; 201266; -.
DR   GeneCards; SLC39A11; -.
DR   HGNC; HGNC:14463; SLC39A11.
DR   HPA; ENSG00000133195; Low tissue specificity.
DR   MIM; 616508; gene.
DR   neXtProt; NX_Q8N1S5; -.
DR   OpenTargets; ENSG00000133195; -.
DR   PharmGKB; PA25581; -.
DR   VEuPathDB; HostDB:ENSG00000133195; -.
DR   eggNOG; KOG2474; Eukaryota.
DR   GeneTree; ENSGT00390000006167; -.
DR   HOGENOM; CLU_015114_1_1_1; -.
DR   InParanoid; Q8N1S5; -.
DR   OMA; MIFVVIE; -.
DR   OrthoDB; 5485028at2759; -.
DR   PhylomeDB; Q8N1S5; -.
DR   TreeFam; TF105905; -.
DR   PathwayCommons; Q8N1S5; -.
DR   SignaLink; Q8N1S5; -.
DR   BioGRID-ORCS; 201266; 10 hits in 1153 CRISPR screens.
DR   ChiTaRS; SLC39A11; human.
DR   GenomeRNAi; 201266; -.
DR   Pharos; Q8N1S5; Tbio.
DR   PRO; PR:Q8N1S5; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8N1S5; Protein.
DR   Bgee; ENSG00000133195; Expressed in bone marrow cell and 173 other cell types or tissues.
DR   ExpressionAtlas; Q8N1S5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005375; F:copper ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0071578; P:zinc ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR003689; ZIP.
DR   PANTHER; PTHR11040:SF210; ZINC TRANSPORTER ZIP11; 1.
DR   PANTHER; PTHR11040; ZINC/IRON TRANSPORTER; 1.
DR   Pfam; PF02535; Zip; 1.
DR   Genevisible; Q8N1S5; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Golgi apparatus;
KW   Ion transport; Membrane; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..342
FT                   /note="Zinc transporter ZIP11"
FT                   /id="PRO_0000308410"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         144..150
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11707075,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028976"
FT   VARIANT         111
FT                   /note="T -> A (in dbSNP:rs2466517)"
FT                   /evidence="ECO:0000269|PubMed:11707075,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_036812"
FT   CONFLICT        113
FT                   /note="A -> T (in Ref. 2; BAC04504)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   342 AA;  35396 MW;  89268838281345D5 CRC64;
     MLQGHSSVFQ ALLGTFFTWG MTAAGAALVF VFSSGQRRIL DGSLGFAAGV MLAASYWSLL
     APAVEMATSS GGFGAFAFFP VAVGFTLGAA FVYLADLLMP HLGAAEDPQT TLALNFGSTL
     MKKKSDPEGP ALLFPESELS IRIGRAGLLS DKSENGEAYQ RKKAAATGLP EGPAVPVPSR
     GNLAQPGGSS WRRIALLILA ITIHNVPEGL AVGVGFGAIE KTASATFESA RNLAIGIGIQ
     NFPEGLAVSL PLRGAGFSTW RAFWYGQLSG MVEPLAGVFG AFAVVLAEPI LPYALAFAAG
     AMVYVVMDDI IPEAQISGNG KLASWASILG FVVMMSLDVG LG
//