ID TRFE_PIG Reviewed; 696 AA. AC P09571; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 04-NOV-2026, entry version 145. DE RecName: Full=Serotransferrin; DE Short=Transferrin; DE AltName: Full=Beta-1 metal-binding globulin; DE AltName: Full=Siderophilin; GN Name=TF; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=3419934; DOI=10.1093/nar/16.17.8720; RA Baldwin G.S., Weinstock J.; RT "Nucleotide sequence of porcine liver transferrin."; RL Nucleic Acids Res. 16:8720-8720(1988). RN [2] RP PROTEIN SEQUENCE OF 1-20. RX PubMed=2065820; RA Chung M.C., Chan S.L., Shimizu S.; RT "Purification of transferrins and lactoferrin using DEAE affi-gel blue."; RL Int. J. Biochem. 23:609-616(1991). RN [3] RP PROTEIN SEQUENCE OF 1-15. RX PubMed=2328566; DOI=10.1016/0305-0491(90)90074-4; RA Baldwin G.S., Bacic T., Chandler R., Grego B., Pedersen J., Simpson R.J., RA Toh B.H., Weinstock J.; RT "Isolation of transferrin from porcine gastric mucosa: comparison with RT porcine serum transferrin."; RL Comp. Biochem. Physiol. 95B:261-268(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=11752780; DOI=10.1107/s0907444901017309; RA Hall D.R., Hadden J.M., Leonard G.A., Bailey S., Neu M., Winn M., RA Lindley P.F.; RT "The crystal and molecular structures of diferric porcine and rabbit serum RT transferrins at resolutions of 2.15 and 2.60 A, respectively."; RL Acta Crystallogr. D 58:70-80(2002). 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. It is responsible for the transport of iron from CC sites of absorption and heme degradation to those of storage and CC utilization. Serum transferrin may also have a further role in CC stimulating cell proliferation. CC -!- SUBUNIT: Monomer. Part of a complex composed of SLC40A1/ferroportin, CC TF/transferrin and HEPH/hephaestin that transfers iron from cells to CC transferrin. {ECO:0000250|UniProtKB:P02787}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. 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; X12386; CAA30943.1; -; mRNA. DR PIR; S01384; S01384. DR PDB; 1H76; X-ray; 2.15 A; A=1-696. DR AlphaFoldDB; P09571; -. DR SMR; P09571; -. DR FunCoup; P09571; 641. DR STRING; 9823.ENSSSCP00000074302; -. DR MEROPS; S60.970; -. DR GlyCosmos; P09571; 2 sites, No reported glycans. DR GlyGen; P09571; 2 sites. DR PaxDb; 9823-ENSSSCP00000074302; -. DR PeptideAtlas; P09571; -. DR eggNOG; ENOG502QT0C; Eukaryota. DR InParanoid; P09571; -. DR OMA; AAKVRWC; -. DR EvolutionaryTrace; P09571; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0005769; C:early endosome; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; 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:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central. DR GO; GO:0051241; P:negative regulation of multicellular organismal process; IEA:UniProtKB-ARBA. DR CDD; cd13617; PBP2_transferrin_C; 1. DR CDD; cd13618; PBP2_transferrin_N; 1. DR FunFam; 3.40.190.10:FF:000095; Lactotransferrin; 1. DR FunFam; 3.40.190.10:FF:000105; Serotransferrin; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4. DR InterPro; IPR030685; Serotransferrin_mammal. DR InterPro; IPR016357; Transferrin. DR InterPro; IPR001156; Transferrin-like_dom. DR InterPro; IPR018195; Transferrin_Fe_BS. DR PANTHER; PTHR11485:SF31; SEROTRANSFERRIN; 1. DR PANTHER; PTHR11485; TRANSFERRIN; 1. DR Pfam; PF00405; Transferrin; 2. DR PIRSF; PIRSF500682; Serotransferrin; 1. 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. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Ion transport; Iron; Iron transport; Metal-binding; Methylation; KW Phosphoprotein; Reference proteome; Repeat; Secreted; Transport. FT CHAIN 1..696 FT /note="Serotransferrin" FT /id="PRO_0000082439" FT DOMAIN 6..332 FT /note="Transferrin-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DOMAIN 346..672 FT /note="Transferrin-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 62 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 94 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 119 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 123 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 125 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 126 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 192 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 253 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 396 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 431 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 458 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 462 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 464 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 465 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 526 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT BINDING 594 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT MOD_RES 23 FT /note="Dimethylated arginine" FT /evidence="ECO:0000250|UniProtKB:P12346" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02787" FT MOD_RES 674 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02787" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 497 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 9..47 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 19..38 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 117..198 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 157..173 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 160..181 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 170..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 231..245 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 343..605 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 349..381 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 359..372 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 406..682 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 423..646 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 456..532 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 480..673 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 490..504 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 501..515 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 572..586 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT DISULFID 624..629 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741" FT VARIANT 308 FT /note="K -> R" FT CONFLICT 20 FT /note="S -> E (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 13..29 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 44..52 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 63..69 FT /evidence="ECO:0007829|PDB:1H76" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 76..85 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 91..101 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 124..128 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 145..152 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:1H76" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 191..200 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 213..217 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 239..244 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 254..261 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 264..278 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 315..319 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 321..331 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 346..351 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 352..365 FT /evidence="ECO:0007829|PDB:1H76" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 369..377 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 378..387 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 392..395 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 397..405 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 409..417 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 431..438 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 447..449 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 463..467 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 468..477 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 482..485 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 486..488 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 499..501 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 525..535 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 538..543 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 546..549 FT /evidence="ECO:0007829|PDB:1H76" FT TURN 558..562 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 568..571 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 577..579 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 580..585 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 588..591 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 595..598 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 603..617 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 634..637 FT /evidence="ECO:0007829|PDB:1H76" FT STRAND 646..649 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 655..659 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 661..669 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 671..673 FT /evidence="ECO:0007829|PDB:1H76" FT HELIX 677..682 FT /evidence="ECO:0007829|PDB:1H76" SQ SEQUENCE 696 AA; 76968 MW; 787C59F42D844B26 CRC64; VAQKTVRWCT ISNQEANKCS SFRENMSKAV KNGPLVSCVK KSSYLDCIKA IRDKEADAVT LDAGLVFEAG LAPYNLKPVV AEFYGQKDNP QTHYYAVAVV KKGSNFQWNQ LQGKRSCHTG LGRSAGWIIP MGLLYDQLPE PRKPIEKAVA SFFSSSCVPC ADPVNFPKLC QQCAGKGAEK CACSNHEPYF GYAGAFNCLK EDAGDVAFVK HSTVLENLPD KADRDQYELL CRDNTRRPVD DYENCYLAQV PSHAVVARSV DGQEDSIWEL LNQAQEHFGR DKSPDFQLFS SSHGKDLLFK DSANGFLKIP SKMDSSLYLG YQYVTALRNL REEISPDSSK NECKKVRWCA IGHEETQKCD AWSINSGGKI ECVSAENTED CIAKIVKGEA DAMSLDGGYI YIAGKCGLVP VLAENYKTEG ENCVNTPEKG YLAVAVVKKS SGPDLNWNNL KGKKSCHTAV DRTAGWNIPM GLLYNKINSC KFDQFFGEGC APGSQRNSSL CALCIGSERA PGRECLANNH ERYYGYTGAF RCLVEKGDVA FVKDQVVQQN TDGKNKDDWA KDLKQMDFEL LCQNGAREPV DNAENCHLAR APNHAVVARD DKVTCVAEEL LKQQAQFGRH VTDCSSSFCM FKSNTKDLLF RDDTQCLARV GKTTYESYLG ADYITAVANL RKCSTSKLLE ACTFHSAKNP RVETTT //