TRFE_GADMO
ID TRFE_GADMO Reviewed; 642 AA.
AC Q92079;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Serotransferrin;
DE Flags: Fragment;
GN Name=tf;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8653583; DOI=10.1016/0305-0491(95)02023-3;
RA Denovan-Wright E.M., Ramsey N.B., McCormick C.J., Lazier C.B., Wright J.M.;
RT "Nucleotide sequence of transferrin cDNAs and tissue-specific of the
RT transferrin gene in Atlantic cod (Gadus morhua).";
RL Comp. Biochem. Physiol. 113B:269-273(1996).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Brain and liver; to a lesser extent in kidney and
CC heart.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; L40370; AAB08440.1; -; mRNA.
DR AlphaFoldDB; Q92079; -.
DR SMR; Q92079; -.
DR STRING; 8049.ENSGMOP00000011156; -.
DR MEROPS; S60.970; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
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; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport;
KW Metal-binding; Reference proteome; Repeat; Secreted; Transport.
FT CHAIN <1..642
FT /note="Serotransferrin"
FT /id="PRO_0000082441"
FT DOMAIN 1..280
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 290..621
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 25
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 54
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 79
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 83
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 85
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 86
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 152
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 208
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 344
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 379
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 404
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 408
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 410
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 411
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 474
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 543
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 121..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 186..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 293..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 303..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 354..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 369..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 402..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 426..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 436..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 447..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 520..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT NON_TER 1
SQ SEQUENCE 642 AA; 67913 MW; F60B98F5ED06C024 CRC64;
GIKEADATEC ILAIKAGEAD AITLDGGEIY TAGQHPYDLQ PIISEKYGSG SSCYYAVAVV
KKDTGFSFKQ LRGKKSCHTG IGKTAGWNIP IGTLLTTGQL VWSGQEDLPV ESVSTFFSKS
CVPGAGGLVG GKLCTLCPSD CSKSATNPYF GYAGAFKCLK DDAGDVAFIN HLTVPASEKA
NYELLCLDGT RAPIDSYKTC NLARVPAHAV VSRVDPELAE RIFTALTTVT GFSFFSSAGF
GAANLMFKDT TQSLVRLPDG SNSFLYLGAK YMASIQSLKK ESDQPITPAI KWCAVGHAEK
KKCDSWSSFS VSDGVKSVAC QISLTVEGCF QRIMRQEADA MSVDGGQVYT AGKCQLIPAM
VEQYNQSLCS SAGTPQATYF AVAVVKKGSG VTWDNLRGKR SCHTGLGRTA GWNIPMGLVH
SIHGSCDFGG FFPSGCAPGS EPSSTFCRQC AGSGSGVEDG SKCSASSVEK YYGYAGAFRC
LVDGAGDVAF IKHTIVADNS DGQGPAWATA LKSSDYQLIC PGGVGRAEIS DFASCNLAAV
PSHAVVTRQD IRDDVVKMLL DQQRKFGIDG SDPLFRIYES KDGNNLLFKD STKCLKEIPS
LTTADAFLGT GYVNAIMSLR QCPETASELE KTCISSSCST AE
