Tag | Content |
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CPLM ID | CPLM-004018 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serotransferrin |
Protein Synonyms/Alias | Transferrin; Beta-1 metal-binding globulin; Liver regeneration-related protein LRRG03; Siderophilin |
Gene Name | Tf |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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26 | AVPDKTVKWCAVSEH | acetylation | [1] | 46 | ISFRDHMKTVLPADG | acetylation | [1] | 134 | QLNQLQGKKSCHTGL | acetylation | [1] | 225 | GGDVAFVKHTTIFEV | acetylation | [1] | 252 | LCLDNTRKPVDQYED | acetylation | [1] | 278 | VARNGDGKEDLIWEI | acetylation | [1] | 295 | VAQEHFGKGKSKDFQ | acetylation | [1] | 299 | HFGKGKSKDFQLFGS | acetylation | [1] | 310 | LFGSPLGKDLLFKDS | acetylation | [1] | 315 | LGKDLLFKDSAFGLL | acetylation | [1] | 466 | SINWNNLKGKKSCHT | acetylation | [1] | 553 | KGDVAFVKHQTVLEN | acetylation | [1] | 564 | VLENTNGKNTAAWAK | acetylation | [1] | 629 | AQKDLFWKGDKDCTG | acetylation | [1] | 646 | CLFRSSTKDLLFRDD | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. |
Sequence Annotation | DOMAIN 25 347 Transferrin-like 1. DOMAIN 360 683 Transferrin-like 2. METAL 82 82 Iron 1 (By similarity). METAL 114 114 Iron 1 (By similarity). METAL 207 207 Iron 1 (By similarity). METAL 268 268 Iron 1 (By similarity). METAL 410 410 Iron 2 (By similarity). METAL 447 447 Iron 2 (By similarity). METAL 536 536 Iron 2 (By similarity). METAL 604 604 Iron 2 (By similarity). BINDING 139 139 Carbonate 1 (By similarity). BINDING 143 143 Carbonate 1 (By similarity). BINDING 145 145 Carbonate 1; via amide nitrogen (By BINDING 146 146 Carbonate 1; via amide nitrogen (By BINDING 473 473 Carbonate 2 (By similarity). BINDING 477 477 Carbonate 2 (By similarity). BINDING 479 479 Carbonate 2; via amide nitrogen (By BINDING 480 480 Carbonate 2; via amide nitrogen (By MOD_RES 42 42 Omega-N-methylated arginine. CARBOHYD 512 512 N-linked (GlcNAc...) (Potential). DISULFID 28 67 By similarity. DISULFID 38 58 By similarity. DISULFID 137 213 By similarity. DISULFID 156 350 By similarity. DISULFID 177 193 By similarity. DISULFID 180 196 By similarity. DISULFID 190 198 By similarity. DISULFID 246 260 By similarity. DISULFID 363 395 By similarity. DISULFID 373 386 By similarity. DISULFID 420 693 By similarity. DISULFID 435 656 By similarity. DISULFID 471 542 By similarity. DISULFID 495 684 By similarity. DISULFID 505 519 By similarity. DISULFID 516 525 By similarity. DISULFID 582 596 By similarity. DISULFID 634 639 By similarity. |
Keyword | Alternative splicing; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding; Methylation; Reference proteome; Repeat; Secreted; Signal; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 698 AA |
Protein Sequence | MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP ADGPRLACVK 60 KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA AEFYGSLEHP QTHYLAVAVV 120 KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC 180 ADPVAFPQLC QLCPGCGCSP TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD 240 QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD 300 FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC PEGSIDSAPV 360 KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV NGEADAMSLD GGHAYIAGQC 420 GLVPVMAENY DISSCTNPQS DVFPKGYYAV AVVKASDSSI NWNNLKGKKS CHTGVDRTAG 480 WNIPMGLLFS RINHCKFDEF FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF 540 QCLVEKGDVA FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ 600 APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF RDDTKCLTKL 660 PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS 698 |
Gene Ontology | GO:0005604; C:basement membrane; IDA:RGD. GO:0005615; C:extracellular space; IDA:RGD. GO:0008199; F:ferric iron binding; IDA:RGD. GO:0015091; F:ferric iron transmembrane transporter activity; IDA:RGD. GO:0006953; P:acute-phase response; IEP:RGD. GO:0006879; P:cellular iron ion homeostasis; TAS:RGD. GO:0071320; P:cellular response to cAMP; IEP:UniProtKB. GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:UniProtKB. GO:0006917; P:induction of apoptosis; ISS:UniProtKB. GO:0031643; P:positive regulation of myelination; IDA:RGD. GO:0001666; P:response to hypoxia; IEP:RGD. |
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