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UniProtKB - P02788 (TRFL_HUMAN)

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Protein

Lactotransferrin

Gene

LTF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate.
Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.
Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.
Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.
Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.
The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.
Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELENOH promoters.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei23PspA1
Binding sitei32PspA1
Metal bindingi79Iron or copper 1PROSITE-ProRule annotation13 Publications1
Active sitei92Curated1
Metal bindingi111Iron or copper 1PROSITE-ProRule annotation13 Publications1
Binding sitei136Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications1
Binding sitei140Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications1
Binding sitei142Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Binding sitei143Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Metal bindingi211Iron or copper 1PROSITE-ProRule annotation13 Publications1
Sitei229Important for iron binding1
Metal bindingi272Iron or copper 1; via tele nitrogenPROSITE-ProRule annotation13 Publications1
Active sitei278NucleophileCurated1
Metal bindingi414Iron or copper 2PROSITE-ProRule annotation13 Publications1
Metal bindingi454Iron or copper 2PROSITE-ProRule annotation13 Publications1
Binding sitei480Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications1
Binding sitei484Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications1
Binding sitei486Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Binding sitei487Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications1
Metal bindingi547Iron or copper 2PROSITE-ProRule annotation13 Publications1
Metal bindingi616Iron or copper 2; via tele nitrogenPROSITE-ProRule annotation13 Publications1

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: CAFA
  • DNA binding Source: UniProtKB-KW
  • heparin binding Source: MGI
  • iron ion binding Source: UniProtKB
  • lipopolysaccharide binding Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: UniProtKB
  • serine-type endopeptidase activity Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • antifungal humoral response Source: UniProtKB
  • antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
  • antimicrobial humoral response Source: Reactome
  • bone morphogenesis Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • humoral immune response Source: ProtInc
  • innate immune response Source: UniProtKB
  • innate immune response in mucosa Source: UniProtKB
  • ion transport Source: UniProtKB-KW
  • iron assimilation by chelation and transport Source: Reactome
  • killing of cells of other organism Source: UniProtKB
  • membrane disruption in other organism Source: UniProtKB
  • negative regulation by host of viral process Source: AgBase
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of ATPase activity Source: AgBase
  • negative regulation of cysteine-type endopeptidase activity Source: CAFA
  • negative regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • negative regulation of membrane potential Source: UniProtKB
  • negative regulation of osteoclast development Source: UniProtKB
  • negative regulation of single-species biofilm formation in or on host organism Source: UniProtKB
  • negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
  • negative regulation of viral genome replication Source: AgBase
  • negative regulation of viral process Source: AgBase
  • neutrophil degranulation Source: Reactome
  • ossification Source: UniProtKB-KW
  • positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
  • positive regulation of chondrocyte proliferation Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: UniProtKB
  • positive regulation of osteoblast proliferation Source: UniProtKB
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
  • regulation of cytokine production Source: UniProtKB
  • regulation of tumor necrosis factor production Source: UniProtKB
  • retina homeostasis Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionAntibiotic, Antimicrobial, DNA-binding, Heparin-binding, Hydrolase, Protease, Serine protease
Biological processImmunity, Ion transport, Iron transport, Osteogenesis, Transcription, Transcription regulation, Transport
LigandIron, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1222449 Mtb iron assimilation by chelation
R-HSA-6798695 Neutrophil degranulation
R-HSA-6799990 Metal sequestration by antimicrobial proteins
R-HSA-6803157 Antimicrobial peptides
R-HSA-977225 Amyloid fiber formation
SIGNORiP02788

Protein family/group databases

MEROPSiS60.001

Names & Taxonomyi

Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
Alternative name(s):
Growth-inhibiting protein 12
Talalactoferrin
Cleaved into the following 5 chains:
Lactoferricin-H
Short name:
Lfcin-H
Kaliocin-1
Lactoferroxin-A
Lactoferroxin-B
Lactoferroxin-C
Gene namesi
Name:LTF
Synonyms:GIG12, LF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000012223.12
HGNCiHGNC:6720 LTF
MIMi150210 gene
neXtProtiNX_P02788

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20 – 23Missing : Abolishes binding to heparin, lipid A, lysozyme and DNA. 1 Publication4
Mutagenesisi20 – 22Missing : Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. 1 Publication3
Mutagenesisi20 – 21Missing : Impairs binding to heparin, lipid A, lysozyme and DNA. 2
Mutagenesisi79D → S: Impairs iron binding and changes domain closure. 1 Publication1
Mutagenesisi92K → A: Almost no protease activity. 1 Publication1
Mutagenesisi140R → D, E or S: Disrupts anion binding site and destabilizes iron binding. 2 Publications1
Mutagenesisi229R → G or E: Destabilizes iron binding slightly. 2 Publications1
Mutagenesisi229R → K or L: Destabilizes iron binding significantly. 2 Publications1
Mutagenesisi270P → V: No effect. 1 Publication1
Mutagenesisi272H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. 1 Publication1
Mutagenesisi278S → A: No protease activity. 1 Publication1

Organism-specific databases

DisGeNETi4057
OpenTargetsiENSG00000012223
PharmGKBiPA30482

Protein family/group databases

Allergomei1384 Hom s LF

Chemistry databases

DrugBankiDB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE
DB03485 Alpha-D-Fucose
DB03017 Lauric Acid
DB04743 Nimesulide
DB03040 Nitrilotriacetic Acid
DB08439 Parecoxib

Polymorphism and mutation databases

BioMutaiLTF
DMDMi85700158

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003573220 – 710LactotransferrinAdd BLAST691
PeptideiPRO_000042277020 – 67Lactoferricin-HAdd BLAST48
PeptideiPRO_0000035733171 – 201Kaliocin-1Add BLAST31
PeptideiPRO_0000035734338 – 343Lactoferroxin-A6
PeptideiPRO_0000035735543 – 547Lactoferroxin-B5
PeptideiPRO_0000035736680 – 686Lactoferroxin-C7

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 64
Disulfide bondi38 ↔ 55
Disulfide bondi134 ↔ 217
Glycosylationi156N-linked (GlcNAc...) asparagine7 Publications1
Disulfide bondi176 ↔ 192
Disulfide bondi189 ↔ 200
Disulfide bondi250 ↔ 264
Disulfide bondi367 ↔ 399
Disulfide bondi377 ↔ 390
Disulfide bondi424 ↔ 705
Disulfide bondi446 ↔ 668
Disulfide bondi478 ↔ 553
Glycosylationi497N-linked (GlcNAc...) asparagine6 Publications1
Disulfide bondi502 ↔ 696
Disulfide bondi512 ↔ 526
Disulfide bondi523 ↔ 536
Disulfide bondi594 ↔ 608
Glycosylationi642N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi646 ↔ 651
Isoform DeltaLf (identifier: P02788-2)
Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391.
Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP02788
PaxDbiP02788
PeptideAtlasiP02788
PRIDEiP02788
ProteomicsDBi12709
51597

PTM databases

GlyConnecti320
iPTMnetiP02788
PhosphoSitePlusiP02788
UniCarbKBiP02788

Expressioni

Tissue specificityi

High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine. In kidney, detected in the distal collecting tubules in the medulla but not in the cortical region or in blood vessels. Detected in peripheral blood neutrophils (at protein level). Isoform 1 and isoform DeltaLf are expressed in breast, prostate, spleen, pancreas, kidney, small intestine, lung, skeletal muscle, uterus, thymus and fetal liver. Isoform 1 is expressed in brain, testis and peripheral blood leukocytes; isoform DeltaLf is barely detectable in these tissues. Isoform DeltaLf is expressed in placenta, liver and ovary; isoform 1 is barely detectable in these tissues. In kidney, isoform 1 is expressed at high levels in the collecting tubules of the medulla but at very low levels in the cortex.3 Publications

Gene expression databases

BgeeiENSG00000012223
ExpressionAtlasiP02788 baseline and differential
GenevisibleiP02788 HS

Organism-specific databases

HPAiCAB008646
CAB016201
HPA057177
HPA059976

Interactioni

Subunit structurei

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1.20 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi110235, 38 interactors
CORUMiP02788
DIPiDIP-41354N
IntActiP02788, 19 interactors
MINTiP02788
STRINGi9606.ENSP00000231751

Structurei

Secondary structure

1710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 31Combined sources8
Helixi32 – 47Combined sources16
Beta strandi50 – 52Combined sources3
Beta strandi53 – 57Combined sources5
Helixi61 – 69Combined sources9
Beta strandi75 – 78Combined sources4
Helixi80 – 87Combined sources8
Turni89 – 91Combined sources3
Beta strandi93 – 102Combined sources10
Beta strandi104 – 118Combined sources15
Beta strandi119 – 121Combined sources3
Helixi125 – 127Combined sources3
Beta strandi132 – 136Combined sources5
Turni141 – 144Combined sources4
Helixi145 – 151Combined sources7
Helixi152 – 154Combined sources3
Turni159 – 161Combined sources3
Helixi164 – 171Combined sources8
Beta strandi172 – 176Combined sources5
Turni182 – 184Combined sources3
Helixi186 – 188Combined sources3
Turni189 – 191Combined sources3
Helixi196 – 198Combined sources3
Beta strandi206 – 208Combined sources3
Helixi210 – 219Combined sources10
Beta strandi224 – 229Combined sources6
Helixi232 – 236Combined sources5
Helixi240 – 243Combined sources4
Beta strandi246 – 250Combined sources5
Turni251 – 253Combined sources3
Beta strandi254 – 257Combined sources4
Helixi258 – 263Combined sources6
Beta strandi266 – 270Combined sources5
Beta strandi273 – 280Combined sources8
Helixi283 – 297Combined sources15
Turni299 – 301Combined sources3
Beta strandi317 – 319Combined sources3
Beta strandi325 – 328Combined sources4
Helixi335 – 339Combined sources5
Helixi341 – 348Combined sources8
Helixi349 – 351Combined sources3
Helixi354 – 362Combined sources9
Beta strandi363 – 370Combined sources8
Helixi371 – 383Combined sources13
Turni384 – 386Combined sources3
Beta strandi387 – 395Combined sources9
Helixi396 – 404Combined sources9
Beta strandi410 – 413Combined sources4
Helixi415 – 423Combined sources9
Beta strandi427 – 434Combined sources8
Beta strandi436 – 439Combined sources4
Beta strandi440 – 442Combined sources3
Helixi446 – 448Combined sources3
Beta strandi454 – 463Combined sources10
Helixi469 – 471Combined sources3
Beta strandi475 – 480Combined sources6
Turni485 – 488Combined sources4
Helixi489 – 499Combined sources11
Helixi504 – 506Combined sources3
Beta strandi508 – 512Combined sources5
Beta strandi514 – 516Combined sources3
Helixi521 – 523Combined sources3
Turni533 – 536Combined sources4
Helixi546 – 555Combined sources10
Beta strandi560 – 565Combined sources6
Helixi566 – 570Combined sources5
Beta strandi573 – 576Combined sources4
Helixi580 – 583Combined sources4
Helixi587 – 589Combined sources3
Beta strandi590 – 593Combined sources4
Beta strandi599 – 601Combined sources3
Helixi602 – 607Combined sources6
Beta strandi610 – 613Combined sources4
Beta strandi617 – 620Combined sources4
Helixi622 – 624Combined sources3
Helixi625 – 639Combined sources15
Beta strandi640 – 642Combined sources3
Turni646 – 649Combined sources4
Beta strandi655 – 657Combined sources3
Beta strandi666 – 670Combined sources5
Helixi678 – 682Combined sources5
Helixi684 – 696Combined sources13
Helixi700 – 709Combined sources10

3D structure databases

DisProtiDP00616
ProteinModelPortaliP02788
SMRiP02788
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02788

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini364 – 695Transferrin-like 2PROSITE-ProRule annotationAdd BLAST332

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 29Bactericidal and antifungal activity10
Regioni20 – 24Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding5
Regioni21 – 22Important for full bactericidal and antifungal activities2
Regioni39 – 49Bactericidal and antifungal activityAdd BLAST11
Regioni39 – 49Interaction with lipopolysaccharideAdd BLAST11
Regioni39 – 46Interaction with pspA8
Regioni46 – 51Involved in glycosaminoglycan binding6
Regioni57 – 58Interaction with pspA2

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IEAI Eukaryota
ENOG410XQ36 LUCA
GeneTreeiENSGT00390000001619
HOVERGENiHBG000055
InParanoidiP02788
KOiK17283
OMAiLRPFLNW
OrthoDBiEOG091G0242
PhylomeDBiP02788
TreeFamiTF324013

Family and domain databases

InterProiView protein in InterPro
IPR030684 Lactotransferrin
IPR016357 Transferrin
IPR001156 Transferrin-like_dom
IPR018195 Transferrin_Fe_BS
PANTHERiPTHR11485:SF33 PTHR11485:SF33, 1 hit
PfamiView protein in Pfam
PF00405 Transferrin, 2 hits
PIRSFiPIRSF500683 Lactotransferrin, 1 hit
PIRSF002549 Transferrin, 1 hit
PRINTSiPR00422 TRANSFERRIN
SMARTiView protein in SMART
SM00094 TR_FER, 2 hits
PROSITEiView protein in PROSITE
PS00205 TRANSFERRIN_LIKE_1, 2 hits
PS00206 TRANSFERRIN_LIKE_2, 2 hits
PS00207 TRANSFERRIN_LIKE_3, 2 hits
PS51408 TRANSFERRIN_LIKE_4, 2 hits

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: P02788-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG 
        60         70         80         90        100
PPVSCIKRDS PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV 
       110        120        130        140        150
YGTERQPRTH YYAVAVVKKG GSFQLNELQG LKSCHTGLRR TAGWNVPIGT 
       160        170        180        190        200
LRPFLNWTGP PEPIEAAVAR FFSASCVPGA DKGQFPNLCR LCAGTGENKC 
       210        220        230        240        250
AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE AERDEYELLC 
       260        270        280        290        300
PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 
       310        320        330        340        350
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL 
       360        370        380        390        400
RKSEEEVAAR RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI 
       410        420        430        440        450
ALVLKGEADA MSLDGGYVYT AGKCGLVPVL AENYKSQQSS DPDPNCVDRP 
       460        470        480        490        500
VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT AVDRTAGWNI PMGLLFNQTG 
       510        520        530        540        550
SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS NERYYGYTGA 
       560        570        580        590        600
FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 
       610        620        630        640        650
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF 
       660        670        680        690        700
CLFQSETKNL LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP 
       710
LLEACEFLRK
Length:710
Mass (Da):78,182
Last modified:January 24, 2006 - v6
Checksum:i0489CABA6D13C098
GO
Isoform DeltaLf (identifier: P02788-2) [UniParc]FASTAAdd to basket
Also known as: Delta-lactoferrin

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Note: Contains a phosphoserine at position 10 (alternate). Contains a O-linked (GlcNAc) serine at position 10 (alternate). O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates DeltaLf transcriptional activity, whereas phosphorylation activates it. Phosphorylation at Ser-10 also promotes proteasomal degradation.1 Publication
Show »
Length:666
Mass (Da):73,161
Checksum:iC498CC5861CA1A12
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14L → P in AAA58656 (Ref. 17) Curated1
Sequence conflicti21R → S in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti21R → S in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti36T → D AA sequence (PubMed:8551695).Curated1
Sequence conflicti49R → C in AAH22347 (PubMed:15489334).Curated1
Sequence conflicti130G → C in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti138L → R in AAH22347 (PubMed:15489334).Curated1
Sequence conflicti140Missing AA sequence (PubMed:6510420).Curated1
Sequence conflicti169Missing AA sequence (PubMed:6510420).Curated1
Sequence conflicti409 – 410DA → NASVLMDSEGGFLAR AA sequence (PubMed:6510420).Curated2
Sequence conflicti415G → E in AAA59511 (Ref. 17) Curated1
Sequence conflicti431A → G in AAA58656 (Ref. 17) Curated1
Sequence conflicti456A → T in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti456A → T in AAH15823 (PubMed:15489334).Curated1
Sequence conflicti487G → A in AAA86665 (PubMed:3477300).Curated1
Sequence conflicti531Q → E AA sequence (PubMed:6510420).Curated1
Sequence conflicti537V → E in AAH15822 (PubMed:15489334).Curated1
Sequence conflicti694K → R AA sequence (PubMed:6510420).Curated1
Sequence conflicti694K → R AA sequence (PubMed:7049727).Curated1

Mass spectrometryi

Molecular mass is 5737.8 Da from positions 20 - 67. Determined by ESI. 1 Publication

Polymorphismi

The sequence shown corresponds to the reference genome sequence and is likely to represent the minor allele, whereas most publications refer to the longer sequence containing variant Arg-22 ins. Insertion of the additional arginine in variant Arg-22 ins creates an N-terminal basic cluster of four arginines, all of which appear to be important for the full functionality of the protein, including bactericidal and antifungal activities as well as binding to glycosaminoglycans, pspA, LPS, lysozyme and DNA.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06929822R → RR Associated with lower plasma lactoferrin concentrations. 14 PublicationsCorresponds to variant dbSNP:rs10662431Ensembl.1
Natural variantiVAR_01350429A → T7 PublicationsCorresponds to variant dbSNP:rs1126477Ensembl.1
Natural variantiVAR_01350547K → R Decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis. 8 PublicationsCorresponds to variant dbSNP:rs1126478Ensembl.1
Natural variantiVAR_013506148I → T1 PublicationCorresponds to variant dbSNP:rs1126479Ensembl.1
Natural variantiVAR_013507422G → C2 PublicationsCorresponds to variant dbSNP:rs1042055Ensembl.1
Natural variantiVAR_013508579E → D6 PublicationsCorresponds to variant dbSNP:rs2073495Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0443081 – 44Missing in isoform DeltaLf. 2 PublicationsAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53961 mRNA Translation: CAA37914.1
U07643 mRNA Translation: AAB60324.1
AF332168 mRNA Translation: AAG48753.1
AY178998 mRNA Translation: AAN75578.2
AY137470 mRNA Translation: AAN11304.1
M73700 Genomic DNA Translation: AAA59479.1
M93150 mRNA Translation: AAA36159.1
AY165046 mRNA Translation: AAN63998.1
AY493417 mRNA Translation: AAS72878.1
EU622050 Genomic DNA Translation: ACC95966.1
AK292813 mRNA Translation: BAF85502.1
AK298035 mRNA Translation: BAH12708.1
AC098613 Genomic DNA No translation available.
BC015822 mRNA Translation: AAH15822.1
BC015823 mRNA Translation: AAH15823.1
BC022347 mRNA Translation: AAH22347.1
S52659 Genomic DNA Translation: AAB24877.1
X52941 mRNA Translation: CAA37116.1
M83202 mRNA Translation: AAA59511.1
M83205 mRNA Translation: AAA58656.1
U95626 Genomic DNA Translation: AAB57795.1
M18642 mRNA Translation: AAA86665.1
CCDSiCCDS33747.1 [P02788-1]
CCDS56251.1 [P02788-2]
PIRiG01394 TFHUL
RefSeqiNP_001186078.1, NM_001199149.1 [P02788-2]
NP_001308050.1, NM_001321121.1
NP_001308051.1, NM_001321122.1
NP_002334.2, NM_002343.5 [P02788-1]
UniGeneiHs.529517

Genome annotation databases

EnsembliENST00000231751; ENSP00000231751; ENSG00000012223 [P02788-1]
ENST00000426532; ENSP00000405719; ENSG00000012223 [P02788-2]
GeneIDi4057
KEGGihsa:4057
UCSCiuc003fzr.4 human [P02788-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Similar proteinsi