UniProtKB - P27590 (UROM_RAT)
Protein
Uromodulin
Gene
Umod
Organism
Rattus norvegicus (Rat)
Status
Functioni
Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability. May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelia.By similarity
In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.By similarity
GO - Molecular functioni
- calcium ion binding Source: InterPro
- extracellular matrix structural constituent Source: GO_Central
- IgG binding Source: RGD
GO - Biological processi
- allantoin metabolic process Source: RGD
- apoptotic process Source: RGD
- apoptotic signaling pathway Source: RGD
- autophagy Source: RGD
- calcium ion homeostasis Source: RGD
- cellular chloride ion homeostasis Source: RGD
- cellular response to unfolded protein Source: RGD
- chaperone-mediated protein folding Source: RGD
- chemical homeostasis Source: RGD
- chemokine metabolic process Source: RGD
- connective tissue replacement Source: RGD
- creatinine homeostasis Source: RGD
- defense response to Gram-negative bacterium Source: RGD
- endoplasmic reticulum organization Source: RGD
- excretion Source: RGD
- gene expression Source: RGD
- glomerular filtration Source: RGD
- heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: RGD
- inflammatory response Source: RGD
- ion homeostasis Source: RGD
- juxtaglomerular apparatus development Source: RGD
- kidney development Source: RGD
- leukocyte cell-cell adhesion Source: RGD
- lipid metabolic process Source: RGD
- loop of Henle development Source: RGD
- metanephric ascending thin limb development Source: RGD
- metanephric distal convoluted tubule development Source: RGD
- metanephric thick ascending limb development Source: RGD
- multicellular organismal homeostasis Source: RGD
- neutrophil migration Source: RGD
- organ or tissue specific immune response Source: RGD
- peptidyl-threonine phosphorylation Source: RGD
- protein localization to vacuole Source: RGD
- protein phosphorylation Source: RGD
- regulation of protein transport Source: RGD
- regulation of urine volume Source: RGD
- renal sodium ion absorption Source: RGD
- renal water homeostasis Source: RGD
- response to drug Source: RGD
- response to endoplasmic reticulum stress Source: RGD
- response to organic substance Source: RGD
- response to unfolded protein Source: RGD
- response to water deprivation Source: RGD
- RNA splicing Source: RGD
- sodium ion homeostasis Source: RGD
- tumor necrosis factor-mediated signaling pathway Source: RGD
- ubiquitin-dependent ERAD pathway Source: RGD
- urate catabolic process Source: RGD
Names & Taxonomyi
Protein namesi | Recommended name: UromodulinAlternative name(s): Tamm-Horsfall urinary glycoprotein Short name: THP Cleaved into the following chain: |
Gene namesi | Name:Umod |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3940, Umod |
Subcellular locationi
Plasma membrane
- Apical cell membrane 1 Publication; GPI-anchor By similarity
- Basolateral cell membrane By similarity; GPI-anchor By similarity
- cilium membrane By similarity
Note: Only a small fraction sorts to the basolateral pole of tubular epithelial cells compared to apical localization. Secreted into urine after cleavage. Colocalizes with NPHP1 and KIF3A.By similarity
Extracellular region or secreted
- Secreted By similarity
Note: Detected in urine.By similarity
Cytoskeleton
- spindle pole Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
Extracellular region or secreted
- extracellular space Source: RGD
Golgi apparatus
- Golgi apparatus Source: RGD
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- basolateral plasma membrane Source: UniProtKB
- ciliary membrane Source: UniProtKB-SubCell
- plasma membrane Source: RGD
Other locations
- anchored component of membrane Source: UniProtKB
- apical part of cell Source: RGD
- cell surface Source: GO_Central
- cilium Source: UniProtKB
- cytoplasmic vesicle Source: RGD
- membrane raft Source: RGD
Keywords - Cellular componenti
Cell membrane, Cell projection, Membrane, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 26 | By similarityAdd BLAST | 26 | |
ChainiPRO_0000041675 | 27 – 615 | UromodulinAdd BLAST | 589 | |
ChainiPRO_0000407912 | 27 – 590 | Uromodulin, secreted formAdd BLAST | 564 | |
PropeptideiPRO_0000041676 | 616 – 644 | Removed in mature formSequence analysisAdd BLAST | 29 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 34 ↔ 43 | PROSITE-ProRule annotation | ||
Disulfide bondi | 37 ↔ 52 | PROSITE-ProRule annotation | ||
Glycosylationi | 40 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 54 ↔ 65 | PROSITE-ProRule annotation | ||
Disulfide bondi | 71 ↔ 84 | PROSITE-ProRule annotation | ||
Glycosylationi | 78 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 79 ↔ 93 | PROSITE-ProRule annotation | ||
Disulfide bondi | 95 ↔ 107 | PROSITE-ProRule annotation | ||
Disulfide bondi | 113 ↔ 127 | PROSITE-ProRule annotation | ||
Disulfide bondi | 121 ↔ 136 | PROSITE-ProRule annotation | ||
Disulfide bondi | 138 ↔ 149 | PROSITE-ProRule annotation | ||
Glycosylationi | 235 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 278 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 300 ↔ 309 | By similarity | ||
Disulfide bondi | 303 ↔ 318 | By similarity | ||
Disulfide bondi | 320 ↔ 350 | By similarity | ||
Glycosylationi | 325 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 338 ↔ 428 | By similarity | ||
Disulfide bondi | 369 ↔ 392 | By similarity | ||
Glycosylationi | 399 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 450 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 509 ↔ 569 | PROSITE-ProRule annotation | ||
Glycosylationi | 516 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 530 ↔ 585 | By similarity | ||
Disulfide bondi | 574 ↔ 581 | By similarity | ||
Lipidationi | 615 | GPI-anchor amidated serineSequence analysis | 1 |
Post-translational modificationi
N-glycosylated.By similarity
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine. This cleavage is catalyzed by HPN.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 590 – 591 | CleavageBy similarity | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, GPI-anchor, LipoproteinProteomic databases
PaxDbi | P27590 |
PRIDEi | P27590 |
PTM databases
GlyGeni | P27590, 8 sites |
Expressioni
Tissue specificityi
Expression restricted to the thick ascending limb of the loop of Henle (TALH).1 Publication
Interactioni
Subunit structurei
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000021027 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 30 – 66 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 67 – 108 | EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 109 – 150 | EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 337 – 592 | ZPPROSITE-ProRule annotationAdd BLAST | 256 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 433 – 456 | Important for secretion and polymerization into filamentsBy similarityAdd BLAST | 24 | |
Regioni | 589 – 592 | Essential for cleavage by HPNBy similarity | 4 | |
Regioni | 601 – 610 | Regulates polymerization into filamentsBy similarity | 10 |
Domaini
The ZP domain mediates polymerization, leading to the formation of long filaments.By similarity
Keywords - Domaini
EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | ENOG502QT6B, Eukaryota |
InParanoidi | P27590 |
OrthoDBi | 665331at2759 |
PhylomeDBi | P27590 |
TreeFami | TF330284 |
Family and domain databases
InterProi | View protein in InterPro IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR024731, EGF_dom IPR009030, Growth_fac_rcpt_cys_sf IPR001507, ZP_dom IPR017977, ZP_dom_CS |
Pfami | View protein in Pfam PF12947, EGF_3, 1 hit PF07645, EGF_CA, 1 hit PF00100, Zona_pellucida, 1 hit |
PRINTSi | PR00023, ZPELLUCIDA |
SMARTi | View protein in SMART SM00181, EGF, 3 hits SM00179, EGF_CA, 2 hits SM00241, ZP, 1 hit |
SUPFAMi | SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 2 hits PS01186, EGF_2, 4 hits PS50026, EGF_3, 3 hits PS01187, EGF_CA, 2 hits PS00682, ZP_1, 1 hit PS51034, ZP_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P27590-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGQLLSLTWL LLVMVVTPWF TVAGANDSPE ARRCSECHDN ATCVLDGVVT
60 70 80 90 100
TCSCQAGFTG DGLVCEDIDE CATPWTHNCS NSICMNTLGS YECSCQDGFR
110 120 130 140 150
LTPGLGCIDV NECTEQGLSN CHSLATCVNT EGSYSCVCPK GYRGDGWYCE
160 170 180 190 200
CSPGFCEPGL DCLPQGPSGK LVCQDPCNVY ETLTEYWRST DYGAGYSCDS
210 220 230 240 250
DMHGWYRFTG QGGVRMAETC VPVLRCNTAA PMWLNGSHPS SREGIVSRTA
260 270 280 290 300
CAHWSDHCCL WSTEIQVKAC PGGFYVYNLT EPPECNLAYC TDPSSVEGTC
310 320 330 340 350
EECGVDEDCV SDNGRWRCQC KQDFNVTDVS LLEHRLECEA NEIKISLSKC
360 370 380 390 400
QLQSLGFMKV FMYLNDRQCS GFSERGERDW MSIVTPARDG PCGTVLRRNE
410 420 430 440 450
THATYSNTLY LASEIIIRDI NIRINFECSY PLDMKVSLKT SLQPMVSALN
460 470 480 490 500
ISLGGTGKFT VQMALFQNPT YTQPYQGPSV MLSTEAFLYV GTMLDGGDLS
510 520 530 540 550
RFVLLMTNCY ATPSSNSTDP VKYFIIQDRC PHTEDTTIQV TENGESSQAR
560 570 580 590 600
FSIQMFRFAG NSDLVYLHCE VYLCDTMSEQ CKPTCSGTRY RSGNFIDQTR
610 620 630 640
VLNLGPITRQ GVQASVSKAA SSNLGFLSIW LLLFLSATLT LMVH
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2JSP1 | A0A0G2JSP1_RAT | Uromodulin | Umod | 644 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 155 | F → S in AAH81814 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 326 | V → I in AAH81814 (PubMed:15489334).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M63510 mRNA Translation: AAA42319.1 S75960 mRNA Translation: AAB33313.1 BC081814 mRNA Translation: AAH81814.1 |
PIRi | A40212 |
RefSeqi | NP_058778.1, NM_017082.1 XP_006230169.1, XM_006230107.2 |
Genome annotation databases
GeneIDi | 25128 |
KEGGi | rno:25128 |
UCSCi | RGD:3940, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M63510 mRNA Translation: AAA42319.1 S75960 mRNA Translation: AAB33313.1 BC081814 mRNA Translation: AAH81814.1 |
PIRi | A40212 |
RefSeqi | NP_058778.1, NM_017082.1 XP_006230169.1, XM_006230107.2 |
3D structure databases
SMRi | P27590 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000021027 |
PTM databases
GlyGeni | P27590, 8 sites |
Proteomic databases
PaxDbi | P27590 |
PRIDEi | P27590 |
Genome annotation databases
GeneIDi | 25128 |
KEGGi | rno:25128 |
UCSCi | RGD:3940, rat |
Organism-specific databases
CTDi | 7369 |
RGDi | 3940, Umod |
Phylogenomic databases
eggNOGi | ENOG502QT6B, Eukaryota |
InParanoidi | P27590 |
OrthoDBi | 665331at2759 |
PhylomeDBi | P27590 |
TreeFami | TF330284 |
Miscellaneous databases
PROi | PR:P27590 |
Family and domain databases
InterProi | View protein in InterPro IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR024731, EGF_dom IPR009030, Growth_fac_rcpt_cys_sf IPR001507, ZP_dom IPR017977, ZP_dom_CS |
Pfami | View protein in Pfam PF12947, EGF_3, 1 hit PF07645, EGF_CA, 1 hit PF00100, Zona_pellucida, 1 hit |
PRINTSi | PR00023, ZPELLUCIDA |
SMARTi | View protein in SMART SM00181, EGF, 3 hits SM00179, EGF_CA, 2 hits SM00241, ZP, 1 hit |
SUPFAMi | SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 2 hits PS01186, EGF_2, 4 hits PS50026, EGF_3, 3 hits PS01187, EGF_CA, 2 hits PS00682, ZP_1, 1 hit PS51034, ZP_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | UROM_RAT | |
Accessioni | P27590Primary (citable) accession number: P27590 Secondary accession number(s): Q642D6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | August 1, 1992 | |
Last modified: | December 2, 2020 | |
This is version 150 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |