TRFM_MOUSE
ID TRFM_MOUSE Reviewed; 738 AA.
AC Q9R0R1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Melanotransferrin {ECO:0000250|UniProtKB:P08582};
DE AltName: Full=Membrane-bound transferrin-like protein p97;
DE Short=MTf;
DE AltName: CD_antigen=CD228;
DE Flags: Precursor;
GN Name=Meltf; Synonyms=Mfi2, Mtf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10542324; DOI=10.1016/s0167-4781(99)00173-6;
RA Nakamasu K., Kawamoto T., Shen M., Gotoh O., Teramoto M., Noshiro M.,
RA Kato Y.;
RT "Membrane-bound transferrin-like protein (MTf): structure, evolution and
RT selective expression during chondrogenic differentiation of mouse embryonic
RT cells.";
RL Biochim. Biophys. Acta 1447:258-264(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11231300; DOI=10.1046/j.1432-1327.2001.02017.x;
RA Nakamasu K., Kawamoto T., Yoshida E., Noshiro M., Matsuda Y., Kato Y.;
RT "Structure and promoter analysis of the mouse membrane-bound transferrin-
RT like protein (MTf) gene.";
RL Eur. J. Biochem. 268:1468-1476(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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: Involved in iron cellular uptake. Seems to be internalized
CC and then recycled back to the cell membrane. Binds a single atom of
CC iron per subunit. Could also bind zinc.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; AB024336; BAA86655.1; -; mRNA.
DR EMBL; AB047799; BAB41139.1; -; Genomic_DNA.
DR EMBL; BC040347; AAH40347.1; -; mRNA.
DR CCDS; CCDS28108.1; -.
DR RefSeq; NP_038928.1; NM_013900.2.
DR AlphaFoldDB; Q9R0R1; -.
DR SMR; Q9R0R1; -.
DR STRING; 10090.ENSMUSP00000023464; -.
DR MEROPS; S60.976; -.
DR GlyGen; Q9R0R1; 3 sites.
DR PhosphoSitePlus; Q9R0R1; -.
DR CPTAC; non-CPTAC-4067; -.
DR jPOST; Q9R0R1; -.
DR MaxQB; Q9R0R1; -.
DR PaxDb; Q9R0R1; -.
DR PRIDE; Q9R0R1; -.
DR ProteomicsDB; 298215; -.
DR Antibodypedia; 1405; 337 antibodies from 33 providers.
DR DNASU; 30060; -.
DR Ensembl; ENSMUST00000023464; ENSMUSP00000023464; ENSMUSG00000022780.
DR GeneID; 30060; -.
DR KEGG; mmu:30060; -.
DR UCSC; uc007yxv.1; mouse.
DR CTD; 4241; -.
DR MGI; MGI:1353421; Meltf.
DR VEuPathDB; HostDB:ENSMUSG00000022780; -.
DR eggNOG; ENOG502QSZB; Eukaryota.
DR GeneTree; ENSGT00940000159265; -.
DR HOGENOM; CLU_011309_3_0_1; -.
DR InParanoid; Q9R0R1; -.
DR OMA; WNVPVGF; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; Q9R0R1; -.
DR TreeFam; TF324013; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 30060; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9R0R1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9R0R1; protein.
DR Bgee; ENSMUSG00000022780; Expressed in vestibular epithelium and 54 other tissues.
DR ExpressionAtlas; Q9R0R1; baseline and differential.
DR Genevisible; Q9R0R1; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; ISO:MGI.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:MGI.
DR InterPro; IPR029773; MTF.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR PANTHER; PTHR11485:SF21; PTHR11485:SF21; 1.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Ion transport;
KW Iron; Iron transport; Lipoprotein; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transport; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..709
FT /note="Melanotransferrin"
FT /id="PRO_0000035741"
FT PROPEP 710..738
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000035742"
FT DOMAIN 23..357
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 366..706
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 78
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 107
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 132
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 138
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 139
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 210
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 279
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 451
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 556
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 625
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08582"
FT LIPID 709
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 36..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 130..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 172..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 186..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 257..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 738 AA; 81293 MW; B5D9BFAB30F4B8B1 CRC64;
MRLLSVTFWL LLSLRTVVCV MEVQWCTISD AEQQKCKDMS EAFQGAGIRP SLLCVQGNSA
DHCVQLIKEQ KADAITLDGG AIYEAGKEHG LKPVVGEVYD QDIGTSYYAV AVVRRNSNVT
INTLKGVKSC HTGINRTVGW NVPVGYLVES GHLSVMGCDV LKAVGDYFGG SCVPGTGETS
HSESLCRLCR GDSSGHNVCD KSPLERYYDY SGAFRCLAEG AGDVAFVKHS TVLENTDGNT
LPSWGKSLMS EDFQLLCRDG SRADITEWRR CHLAKVPAHA VVVRGDMDGG LIFQLLNEGQ
LLFSHEDSSF QMFSSKAYSQ KNLLFKDSTL ELVPIATQNY EAWLGQEYLQ AMKGLLCDPN
RLPHYLRWCV LSAPEIQKCG DMAVAFSRQN LKPEIQCVSA ESPEHCMEQI QAGHTDAVTL
RGEDIYRAGK VYGLVPAAGE LYAEEDRSNS YFVVAVARRD SSYSFTLDEL RGKRSCHPYL
GSPAGWEVPI GSLIQRGFIR PKDCDVLTAV SQFFNASCVP VNNPKNYPSA LCALCVGDEK
GRNKCVGSSQ ERYYGYSGAF RCLVEHAGDV AFVKHTTVFE NTNGHNPEPW ASHLRWQDYE
LLCPNGARAE VDQFQACNLA QMPSHAVMVR PDTNIFTVYG LLDKAQDLFG DDHNKNGFQM
FDSSKYHSQD LLFKDATVRA VPVREKTTYL DWLGPDYVVA LEGMLSQQCS GAGAAVQRVP
LLALLLLTLA AGLLPRVL
