Slc39a5
entrez
72002
canonical
uniprot
Q9D856
canonical
ensembl
ENSMUSG00000039878
resolver
ensp
ENSMUSP00000037753
resolver
ensp
ENSMUSP00000131736
resolver
ensp
ENSMUSP00000351708
resolver
enst
ENSMUST00000042666
resolver
enst
ENSMUST00000167859
resolver
genesymbol
Slc39a5
resolver
genesymbol_syn
Zip5
resolver
uniprot
Q9D909
resolver
uniprot_entry
S39A5_MOUSE
resolver
uniprot_sec
Q9D909
resolver
amino_acid_sequence
MGPPVHHLLTGLCVGVALGWVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGHHEPPTGRAAPTSGDNFTHRLQEPELSVDIWAGMPLGPSGWGDQEESKAPDLHGSGPSSLDLFQRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPVAPLTPRQFALLCPALLYQIDSRVCIKTPAPAPPGDVLSALLHSGLAVLFLSLPAPLSLLLLRLLGPRLLRPVLGFLGALAVGTLCGDALLHLLPHAQGGRHTGPSEQSEEDLGPGLSVLGGLFLLFMLENTLGLVRHRGLRPRCCRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEHRGGSIAWMVLLGDCLHNLTDGLALGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQEGLSFRKLLLLSLVSGALGLGGAALGVGLSLGPVPLTPWVFGTTAGVFLYVALVDMLPTLLRPPEPLPVFHVLLQGLGLLLGGSLMFTIALLEEQLVPTVPDG
uniprot
proteins
function
FUNCTION: Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine (PubMed:15322118, PubMed:24303081). The transport mechanism is temperature- and concentration-dependent and saturable (PubMed:15322118). In addition, is also a high affinity copper transporter in vitro (By similarity). Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (PubMed:30324491). Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (By similarity). Plays a role in eye development (By similarity). {ECO:0000250|UniProtKB:Q6ZMH5, ECO:0000269|PubMed:15322118, ECO:0000269|PubMed:24303081, ECO:0000269|PubMed:30324491}.
uniprot
proteins
mass_dalton
56275
uniprot
proteins
post_translational_modification
PTM: N-Glycosylated. {ECO:0000269|PubMed:15322118, ECO:0000269|PubMed:24039764}.; PTM: Methylated at His-371 by METTL9. {ECO:0000250|UniProtKB:Q6ZMH5}.
uniprot
proteins
protein_family
ZIP transporter (TC 2.A.5) family
uniprot
proteins
pubmed
15322118
uniprot
proteins
pubmed
15358787
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18020946
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24039764
uniprot
proteins
pubmed
24303081
uniprot
proteins
pubmed
24891338
uniprot
proteins
pubmed
30324491
uniprot
proteins
sequence_length
535
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:15322118, ECO:0000269|PubMed:15358787, ECO:0000269|PubMed:18020946}; Multi-pass membrane protein {ECO:0000269|PubMed:15322118}. Note=Localized to the basolateral surfaces of enterocytes, pancreatic acinar and endoderm cells (PubMed:15358787). During zinc deficiency diet, the basolateral cell membrane localization is lost in the intestine, the visceral yolk sac and acinar cell (PubMed:15358787). During zinc repletion, is relocalized to the basolateral membrane of enterocytes, visceral endoderm cells and pancreatic acinar cells (PubMed:18020946). Zinc can regulate the turnover of protein at the membrane (PubMed:18020946). During zinc deficiency, is internalized and degraded in enterocytes, acinar cells and endoderm cells (PubMed:18020946). Endocytosed through the endolysosomal degradation pathway RAB5A pathway (PubMed:24039764). {ECO:0000269|PubMed:15358787, ECO:0000269|PubMed:18020946, ECO:0000269|PubMed:24039764}.
uniprot
proteins
transmembrane_region
TRANSMEM 211..231; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 243..263; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 286..306; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 440..460; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 466..486; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 504..524; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins