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 27-MAR-2024, entry version 165. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9R0R1; 3 sites, No reported glycans. DR GlyGen; Q9R0R1; 3 sites. DR PhosphoSitePlus; Q9R0R1; -. DR SwissPalm; Q9R0R1; -. DR CPTAC; non-CPTAC-4067; -. DR jPOST; Q9R0R1; -. DR MaxQB; Q9R0R1; -. DR PaxDb; 10090-ENSMUSP00000023464; -. DR ProteomicsDB; 298215; -. DR Pumba; Q9R0R1; -. DR Antibodypedia; 1405; 407 antibodies from 33 providers. DR DNASU; 30060; -. DR Ensembl; ENSMUST00000023464.6; ENSMUSP00000023464.6; ENSMUSG00000022780.6. DR GeneID; 30060; -. DR KEGG; mmu:30060; -. DR UCSC; uc007yxv.1; mouse. DR AGR; MGI:1353421; -. 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; VNEMLQT; -. DR OrthoDB; 2906687at2759; -. 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 78 CRISPR screens. DR PRO; PR:Q9R0R1; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q9R0R1; Protein. DR Bgee; ENSMUSG00000022780; Expressed in vestibular epithelium and 55 other cell types or tissues. DR ExpressionAtlas; Q9R0R1; baseline and differential. 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; ISO:MGI. DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; ISO:MGI. 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 CDD; cd13529; PBP2_transferrin; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4. DR InterPro; IPR016357; Transferrin. DR InterPro; IPR001156; Transferrin-like_dom. DR InterPro; IPR018195; Transferrin_Fe_BS. DR PANTHER; PTHR11485:SF21; MELANOTRANSFERRIN; 1. DR PANTHER; PTHR11485; TRANSFERRIN; 1. DR Pfam; PF00405; Transferrin; 2. DR PIRSF; PIRSF002549; Transferrin; 1. DR PRINTS; PR00422; TRANSFERRIN. DR SMART; SM00094; TR_FER; 2. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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. DR Genevisible; Q9R0R1; MM. 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 //