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Protein

Zinc transporter ZIP5

Gene

SLC39A5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in polarized cells by carrying out serosal-to-mucosal zinc transport. Plays a role in eye development. Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (PubMed:24891338). Seems to play a central role in controlling organismal zinc status (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport, Zinc transport

Keywords - Ligandi

Zinc

Enzyme and pathway databases

ReactomeiR-HSA-442380. Zinc influx into cells by the SLC39 gene family.

Protein family/group databases

TCDBi2.A.5.4.10. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc transporter ZIP5
Alternative name(s):
Solute carrier family 39 member 5
Zrt- and Irt-like protein 5
Short name:
ZIP-5
Gene namesi
Name:SLC39A5
Synonyms:ZIP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20502. SLC39A5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 212192ExtracellularBy similarityAdd
BLAST
Transmembranei213 – 23321HelicalSequence analysisAdd
BLAST
Topological domaini234 – 24411CytoplasmicSequence analysisAdd
BLAST
Transmembranei245 – 26521HelicalSequence analysisAdd
BLAST
Topological domaini266 – 28722ExtracellularSequence analysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence analysisAdd
BLAST
Topological domaini309 – 444136CytoplasmicSequence analysisAdd
BLAST
Transmembranei445 – 46521HelicalSequence analysisAdd
BLAST
Topological domaini466 – 4705ExtracellularSequence analysis
Transmembranei471 – 49121HelicalSequence analysisAdd
BLAST
Topological domaini492 – 50817CytoplasmicSequence analysisAdd
BLAST
Transmembranei509 – 52921HelicalSequence analysisAdd
BLAST
Topological domaini530 – 54011ExtracellularBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Myopia 24, autosomal dominant (MYP24)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.
See also OMIM:615946
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041M → T in MYP24; affects the BMP/TGF-beta pathway by suppressing expression of SMAD1; loss of function mutation. 1 Publication
Corresponds to variant rs587777625 [ dbSNP | Ensembl ].
VAR_071911
Natural varianti413 – 4131G → A in MYP24; unknown pathological significance. 1 Publication
VAR_074009

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiSLC39A5.
MIMi615946. phenotype.
PharmGKBiPA134872687.

Polymorphism and mutation databases

BioMutaiSLC39A5.
DMDMi332278218.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 540520Zinc transporter ZIP5PRO_0000045795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence analysis
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis
Modified residuei336 – 3361PhosphoserineBy similarity

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ6ZMH5.
PaxDbiQ6ZMH5.
PeptideAtlasiQ6ZMH5.
PRIDEiQ6ZMH5.
TopDownProteomicsiQ6ZMH5.

PTM databases

iPTMnetiQ6ZMH5.
PhosphoSiteiQ6ZMH5.

Expressioni

Tissue specificityi

Expressed in liver, kidney, pancreas, small intestine, colon, spleen, fetal liver and fetal kidney.1 Publication

Gene expression databases

BgeeiQ6ZMH5.
CleanExiHS_SLC39A5.
ExpressionAtlasiQ6ZMH5. baseline and differential.
GenevisibleiQ6ZMH5. HS.

Organism-specific databases

HPAiHPA018423.

Interactioni

Protein-protein interaction databases

BioGridi129541. 45 interactions.
STRINGi9606.ENSP00000266980.

Structurei

3D structure databases

ProteinModelPortaliQ6ZMH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2693. Eukaryota.
COG0428. LUCA.
GeneTreeiENSGT00760000119115.
HOGENOMiHOG000132930.
HOVERGENiHBG084379.
InParanoidiQ6ZMH5.
KOiK14711.
OMAiENGSGMA.
PhylomeDBiQ6ZMH5.
TreeFamiTF318470.

Family and domain databases

InterProiIPR003689. ZIP.
[Graphical view]
PfamiPF02535. Zip. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6ZMH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMGSPVSHLL AGFCVWVVLG WVGGSVPNLG PAEQEQNHYL AQLFGLYGEN
60 70 80 90 100
GTLTAGGLAR LLHSLGLGRV QGLRLGQHGP LTGRAASPAA DNSTHRPQNP
110 120 130 140 150
ELSVDVWAGM PLGPSGWGDL EESKAPHLPR GPAPSGLDLL HRLLLLDHSL
160 170 180 190 200
ADHLNEDCLN GSQLLVNFGL SPAAPLTPRQ FALLCPALLY QIDSRVCIGA
210 220 230 240 250
PAPAPPGDLL SALLQSALAV LLLSLPSPLS LLLLRLLGPR LLRPLLGFLG
260 270 280 290 300
ALAVGTLCGD ALLHLLPHAQ EGRHAGPGGL PEKDLGPGLS VLGGLFLLFV
310 320 330 340 350
LENMLGLLRH RGLRPRCCRR KRRNLETRNL DPENGSGMAL QPLQAAPEPG
360 370 380 390 400
AQGQREKNSQ HPPALAPPGH QGHSHGHQGG TDITWMVLLG DGLHNLTDGL
410 420 430 440 450
AIGAAFSDGF SSGLSTTLAV FCHELPHELG DFAMLLQSGL SFRRLLLLSL
460 470 480 490 500
VSGALGLGGA VLGVGLSLGP VPLTPWVFGV TAGVFLYVAL VDMLPALLRP
510 520 530 540
PEPLPTPHVL LQGLGLLLGG GLMLAITLLE ERLLPVTTEG
Length:540
Mass (Da):56,461
Last modified:May 3, 2011 - v3
Checksum:i171DF129FF5720D1
GO

Sequence cautioni

The sequence AAH27884.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG36005.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041M → T in MYP24; affects the BMP/TGF-beta pathway by suppressing expression of SMAD1; loss of function mutation. 1 Publication
Corresponds to variant rs587777625 [ dbSNP | Ensembl ].
VAR_071911
Natural varianti413 – 4131G → A in MYP24; unknown pathological significance. 1 Publication
VAR_074009

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172768 mRNA. Translation: BAD18751.1.
AK313188 mRNA. Translation: BAG36005.1. Different initiation.
BC027884 mRNA. Translation: AAH27884.1. Different initiation.
CCDSiCCDS8912.2.
RefSeqiNP_001128667.1. NM_001135195.1.
NP_775867.2. NM_173596.2.
XP_005268860.1. XM_005268803.1.
XP_011536500.1. XM_011538198.1.
XP_011536501.1. XM_011538199.1.
XP_011536502.1. XM_011538200.1.
XP_011536503.1. XM_011538201.1.
UniGeneiHs.591018.

Genome annotation databases

EnsembliENST00000266980; ENSP00000266980; ENSG00000139540.
ENST00000454355; ENSP00000405360; ENSG00000139540.
GeneIDi283375.
KEGGihsa:283375.
UCSCiuc010sqj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK172768 mRNA. Translation: BAD18751.1.
AK313188 mRNA. Translation: BAG36005.1. Different initiation.
BC027884 mRNA. Translation: AAH27884.1. Different initiation.
CCDSiCCDS8912.2.
RefSeqiNP_001128667.1. NM_001135195.1.
NP_775867.2. NM_173596.2.
XP_005268860.1. XM_005268803.1.
XP_011536500.1. XM_011538198.1.
XP_011536501.1. XM_011538199.1.
XP_011536502.1. XM_011538200.1.
XP_011536503.1. XM_011538201.1.
UniGeneiHs.591018.

3D structure databases

ProteinModelPortaliQ6ZMH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129541. 45 interactions.
STRINGi9606.ENSP00000266980.

Protein family/group databases

TCDBi2.A.5.4.10. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

PTM databases

iPTMnetiQ6ZMH5.
PhosphoSiteiQ6ZMH5.

Polymorphism and mutation databases

BioMutaiSLC39A5.
DMDMi332278218.

Proteomic databases

MaxQBiQ6ZMH5.
PaxDbiQ6ZMH5.
PeptideAtlasiQ6ZMH5.
PRIDEiQ6ZMH5.
TopDownProteomicsiQ6ZMH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266980; ENSP00000266980; ENSG00000139540.
ENST00000454355; ENSP00000405360; ENSG00000139540.
GeneIDi283375.
KEGGihsa:283375.
UCSCiuc010sqj.3. human.

Organism-specific databases

CTDi283375.
GeneCardsiSLC39A5.
HGNCiHGNC:20502. SLC39A5.
HPAiHPA018423.
MalaCardsiSLC39A5.
MIMi608730. gene.
615946. phenotype.
neXtProtiNX_Q6ZMH5.
PharmGKBiPA134872687.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2693. Eukaryota.
COG0428. LUCA.
GeneTreeiENSGT00760000119115.
HOGENOMiHOG000132930.
HOVERGENiHBG084379.
InParanoidiQ6ZMH5.
KOiK14711.
OMAiENGSGMA.
PhylomeDBiQ6ZMH5.
TreeFamiTF318470.

Enzyme and pathway databases

ReactomeiR-HSA-442380. Zinc influx into cells by the SLC39 gene family.

Miscellaneous databases

GenomeRNAii283375.
PROiQ6ZMH5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZMH5.
CleanExiHS_SLC39A5.
ExpressionAtlasiQ6ZMH5. baseline and differential.
GenevisibleiQ6ZMH5. HS.

Family and domain databases

InterProiIPR003689. ZIP.
[Graphical view]
PfamiPF02535. Zip. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon and Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  3. "The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells."
    Wang F., Kim B.-E., Petris M.J., Eide D.J.
    J. Biol. Chem. 279:51433-51441(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: FUNCTION, VARIANT MYP24 THR-304, CHARACTERIZATION VARIANT MYP24 THR-304.
  5. "Detection of mutations in LRPAP1, CTSH, LEPREL1, ZNF644, SLC39A5, and SCO2 in 298 families with early-onset high myopia by exome sequencing."
    Jiang D., Li J., Xiao X., Li S., Jia X., Sun W., Guo X., Zhang Q.
    Invest. Ophthalmol. Vis. Sci. 56:339-345(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MYP24 ALA-413.

Entry informationi

Entry nameiS39A5_HUMAN
AccessioniPrimary (citable) accession number: Q6ZMH5
Secondary accession number(s): B2R808, Q8N6Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: May 3, 2011
Last modified: July 6, 2016
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.