TRFM_RABIT
ID TRFM_RABIT Reviewed; 736 AA.
AC O97490;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Melanotransferrin {ECO:0000250|UniProtKB:P08582};
DE AltName: Full=Membrane-bound transferrin-like protein p97;
DE AltName: CD_antigen=CD228;
DE Flags: Precursor;
GN Name=MELTF {ECO:0000250|UniProtKB:P08582}; Synonyms=MFI2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9780225; DOI=10.1046/j.1432-1327.1998.2560503.x;
RA Kawamoto T., Pan H., Yan W., Ishida H., Usui E., Oda R., Nakamasu K.,
RA Noshiro M., Kawashima-Ohya Y., Fujii M., Shintani H., Okada Y., Kato Y.;
RT "Expression of membrane-bound transferrin-like protein p97 on the cell
RT surface of chondrocyte.";
RL Eur. J. Biochem. 256:503-509(1998).
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 (By similarity). {ECO:0000250}.
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; AB010995; BAA33956.1; -; mRNA.
DR RefSeq; NP_001075461.1; NM_001081992.1.
DR AlphaFoldDB; O97490; -.
DR SMR; O97490; -.
DR STRING; 9986.ENSOCUP00000011582; -.
DR MEROPS; S60.976; -.
DR PRIDE; O97490; -.
DR GeneID; 100008603; -.
DR KEGG; ocu:100008603; -.
DR CTD; 4241; -.
DR eggNOG; ENOG502QSZB; Eukaryota.
DR InParanoid; O97490; -.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
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; 1.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1.
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;
KW Reference proteome; Repeat; Signal; Transport; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..711
FT /note="Melanotransferrin"
FT /id="PRO_0000035743"
FT PROPEP 712..736
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000035744"
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 625
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT LIPID 711
FT /note="GPI-anchor amidated glycine"
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 736 AA; 80170 MW; F389D9F8A6AC90FC CRC64;
MRCRSAAMWI FLALRTALGS VEVRWCTASE PEQQKCEDMS QAFREAGLQP ALLCVQGTSA
DHCVQLIAAH EADAITLDGG AIYEAGKEHG LKPVVGEVYD QEVGTSYYAV AVVKRSSNVT
INTLRGVKSC HTGINRTVGW NVPVGYLVDS GRLSVMGCDV LKAVSEYFGG SCVPGAGETR
YSESLCRLCR GDTSGEGVCD KSPLERYYDY SGAFRCLAEG AGDVAFVKHS TVLENTDGRT
LPSWGHMLMS RDFELLCRDG SRASVTEWQH CHLARVPAHA VVVRADTDAG LIFRLLNEGQ
RLFSHEGSSF QMFSSEAYGQ KNLLFKDSTL ELVPIATQTY EAWLGPEYLH AMKGLLCDPN
RLPPYLRWCV LSTPEIQKCG DMAVAFSRQR LKPEIQCVSA ESPQHCMEQI QAGHIDAVTL
NGEDIHTAGK TYGLIPAAGE LYAADDRSNS YFVVAVVKRD SAYAFTVDEL RGKRSCHPGF
GSPAGWDVPV GALIHWGYIR PRNCDVLTAV GQFFNASCVP VNNPKKYPSS LCALCVGDEQ
GRNKCTGNSQ ERYYGDSGAF RCLVEGAGDV AFVKHTTIFD NTNGHNPEPW AAHLRSQDYE
LLCPNGARAE AHQFAACNLA QIPSHAVMVR PDTNIFTVYG LLDKAQDLFG DDHNKNGFKM
FDSSSYHGRD LLFKDATVRA VPVGERTTYQ DWLGPDYVAA LEGMQSQRCS GAAVGAPGAS
LLPLLPLAVG LLLSSL
