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Uromodulin (Tamm-Horsfall urinary glycoprotein) (THP) [Cleaved into: Uromodulin, secreted form]

 UROM_RAT                Reviewed;         644 AA.
P27590; Q642D6;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
22-NOV-2017, entry version 142.
RecName: Full=Uromodulin;
AltName: Full=Tamm-Horsfall urinary glycoprotein;
Short=THP;
Contains:
RecName: Full=Uromodulin, secreted form;
Flags: Precursor;
Name=Umod;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1531535; DOI=10.1073/pnas.89.4.1189;
Fukuoka S., Freedman S.D., Yu H., Sukhatme V.P., Scheele G.A.;
"GP-2/THP gene family encodes self-binding
glycosylphosphatidylinositol-anchored proteins in apical secretory
compartments of pancreas and kidney.";
Proc. Natl. Acad. Sci. U.S.A. 89:1189-1193(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7531049;
Yu H., Papa F., Sukhatme V.P.;
"Bovine and rodent Tamm-Horsfall protein (THP) genes: cloning,
structural analysis, and promoter identification.";
Gene Expr. 4:63-75(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=379435;
Hoyer J.R., Sisson S.P., Vernier R.L.;
"Tamm-Horsfall glycoprotein: ultrastructural immunoperoxidase
localization in rat kidney.";
Lab. Invest. 41:168-173(1979).
-!- FUNCTION: Uromodulin: 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.
{ECO:0000250|UniProtKB:P07911}.
-!- FUNCTION: Uromodulin, secreted form: 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. {ECO:0000250|UniProtKB:Q91X17}.
-!- SUBUNIT: Uromodulin, secreted form: homodimer that then
polymerizes into long filaments. {ECO:0000250|UniProtKB:P07911}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:379435}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P07911}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P07911}. Cell projection, cilium membrane
{ECO:0000250|UniProtKB:P07911}. 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. {ECO:0000250|UniProtKB:P07911}.
-!- SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted
{ECO:0000250|UniProtKB:P07911}. Note=Detected in urine.
{ECO:0000250|UniProtKB:P07911}.
-!- TISSUE SPECIFICITY: Expression restricted to the thick ascending
limb of the loop of Henle (TALH). {ECO:0000269|PubMed:379435}.
-!- DOMAIN: The ZP domain mediates polymerization, leading to the
formation of long filaments. {ECO:0000250|UniProtKB:P07911}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07911}.
-!- PTM: Proteolytically cleaved at a conserved C-terminal proteolytic
cleavage site to generate the secreted form found in urine. This
cleavage is catalyzed by HPN. {ECO:0000250|UniProtKB:P07911}.
-----------------------------------------------------------------------
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EMBL; M63510; AAA42319.1; -; mRNA.
EMBL; S75960; AAB33313.1; -; mRNA.
EMBL; BC081814; AAH81814.1; -; mRNA.
PIR; A40212; A40212.
RefSeq; NP_058778.1; NM_017082.1.
RefSeq; XP_006230169.1; XM_006230107.2.
UniGene; Rn.31982; -.
ProteinModelPortal; P27590; -.
SMR; P27590; -.
STRING; 10116.ENSRNOP00000021027; -.
PaxDb; P27590; -.
PRIDE; P27590; -.
GeneID; 25128; -.
KEGG; rno:25128; -.
UCSC; RGD:3940; rat.
CTD; 7369; -.
RGD; 3940; Umod.
eggNOG; ENOG410IVSV; Eukaryota.
eggNOG; ENOG410YDU6; LUCA.
HOGENOM; HOG000293303; -.
HOVERGEN; HBG004349; -.
InParanoid; P27590; -.
KO; K18274; -.
PhylomeDB; P27590; -.
TreeFam; TF330284; -.
PRO; PR:P27590; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005929; C:cilium; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019864; F:IgG binding; ISO:RGD.
GO; GO:0048878; P:chemical homeostasis; ISO:RGD.
GO; GO:0007588; P:excretion; ISO:RGD.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0072218; P:metanephric ascending thin limb development; ISO:RGD.
GO; GO:0072221; P:metanephric distal convoluted tubule development; ISO:RGD.
GO; GO:0072233; P:metanephric thick ascending limb development; ISO:RGD.
GO; GO:1990266; P:neutrophil migration; ISO:RGD.
GO; GO:2000021; P:regulation of ion homeostasis; ISO:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024731; EGF_dom.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00023; ZPELLUCIDA.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00241; ZP; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
2: Evidence at transcript level;
Cell membrane; Cell projection; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 26 {ECO:0000250|UniProtKB:P07911}.
CHAIN 27 615 Uromodulin.
/FTId=PRO_0000041675.
CHAIN 27 590 Uromodulin, secreted form.
/FTId=PRO_0000407912.
PROPEP 616 644 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000041676.
DOMAIN 30 66 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 67 108 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 109 150 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 337 592 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
REGION 433 456 Important for secretion and
polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
REGION 589 592 Essential for cleavage by HPN.
{ECO:0000250|UniProtKB:P07911}.
REGION 601 610 Regulates polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
SITE 590 591 Cleavage. {ECO:0000250|UniProtKB:P07911}.
LIPID 615 615 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 516 516 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 43 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 37 52 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 54 65 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 71 84 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 79 93 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 95 107 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 113 127 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 121 136 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 138 149 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 300 309 {ECO:0000250|UniProtKB:P07911}.
DISULFID 303 318 {ECO:0000250|UniProtKB:P07911}.
DISULFID 320 350 {ECO:0000250|UniProtKB:P07911}.
DISULFID 338 428 {ECO:0000250|UniProtKB:P07911}.
DISULFID 369 392 {ECO:0000250|UniProtKB:P07911}.
DISULFID 509 569 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 530 585 {ECO:0000250|UniProtKB:P07911}.
DISULFID 574 581 {ECO:0000250|UniProtKB:P07911}.
CONFLICT 155 155 F -> S (in Ref. 3; AAH81814).
{ECO:0000305}.
CONFLICT 326 326 V -> I (in Ref. 3; AAH81814).
{ECO:0000305}.
SEQUENCE 644 AA; 71062 MW; D26DB419C669826A CRC64;
MGQLLSLTWL LLVMVVTPWF TVAGANDSPE ARRCSECHDN ATCVLDGVVT TCSCQAGFTG
DGLVCEDIDE CATPWTHNCS NSICMNTLGS YECSCQDGFR LTPGLGCIDV NECTEQGLSN
CHSLATCVNT EGSYSCVCPK GYRGDGWYCE CSPGFCEPGL DCLPQGPSGK LVCQDPCNVY
ETLTEYWRST DYGAGYSCDS DMHGWYRFTG QGGVRMAETC VPVLRCNTAA PMWLNGSHPS
SREGIVSRTA CAHWSDHCCL WSTEIQVKAC PGGFYVYNLT EPPECNLAYC TDPSSVEGTC
EECGVDEDCV SDNGRWRCQC KQDFNVTDVS LLEHRLECEA NEIKISLSKC QLQSLGFMKV
FMYLNDRQCS GFSERGERDW MSIVTPARDG PCGTVLRRNE THATYSNTLY LASEIIIRDI
NIRINFECSY PLDMKVSLKT SLQPMVSALN ISLGGTGKFT VQMALFQNPT YTQPYQGPSV
MLSTEAFLYV GTMLDGGDLS RFVLLMTNCY ATPSSNSTDP VKYFIIQDRC PHTEDTTIQV
TENGESSQAR FSIQMFRFAG NSDLVYLHCE VYLCDTMSEQ CKPTCSGTRY RSGNFIDQTR
VLNLGPITRQ GVQASVSKAA SSNLGFLSIW LLLFLSATLT LMVH


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