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

 UROM_CANLF              Reviewed;         642 AA.
Q862Z3;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
22-NOV-2017, entry version 100.
RecName: Full=Uromodulin;
AltName: Full=Tamm-Horsfall urinary glycoprotein;
Short=THP;
Contains:
RecName: Full=Uromodulin, secreted form;
Flags: Precursor;
Name=UMOD;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12751332; DOI=10.1080/1042517021000056943;
Cox M.L., Quignon P., Galibert F., Lees G.E., Murphy K.E.;
"Sequencing and radiation hybrid mapping of canine uromodulin.";
DNA Seq. 14:61-69(2003).
[2]
TISSUE SPECIFICITY.
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).
-!- 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:0000250|UniProtKB:P07911}; 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: Detected in kidney and pancreas.
{ECO:0000269|PubMed:1531535}.
-!- 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; AF498324; AAO33163.1; -; mRNA.
UniGene; Cfa.4; -.
ProteinModelPortal; Q862Z3; -.
SMR; Q862Z3; -.
STRING; 9615.ENSCAFP00000026625; -.
PaxDb; Q862Z3; -.
eggNOG; ENOG410IVSV; Eukaryota.
eggNOG; ENOG410YDU6; LUCA.
HOGENOM; HOG000293303; -.
HOVERGEN; HBG004349; -.
InParanoid; Q862Z3; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF07645; EGF_CA; 2.
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; 3.
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 27 620 Uromodulin.
/FTId=PRO_0000041669.
CHAIN 27 588 Uromodulin, secreted form.
/FTId=PRO_0000407908.
PROPEP 621 642 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000041670.
DOMAIN 32 64 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 67 109 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 110 151 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 335 590 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
REGION 431 454 Important for secretion and
polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
REGION 587 590 Essential for cleavage by HPN.
{ECO:0000250|UniProtKB:P07911}.
REGION 599 608 Regulates polymerization into filaments.
{ECO:0000250|UniProtKB:P07911}.
SITE 588 589 Cleavage. {ECO:0000250|UniProtKB:P07911}.
LIPID 620 620 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 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 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 85 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 79 94 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 96 108 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 114 128 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 122 137 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 139 150 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 299 308 {ECO:0000250|UniProtKB:P07911}.
DISULFID 302 317 {ECO:0000250|UniProtKB:P07911}.
DISULFID 319 348 {ECO:0000250|UniProtKB:P07911}.
DISULFID 336 426 {ECO:0000250|UniProtKB:P07911}.
DISULFID 367 390 {ECO:0000250|UniProtKB:P07911}.
DISULFID 507 567 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 528 583 {ECO:0000250|UniProtKB:P07911}.
DISULFID 572 579 {ECO:0000250|UniProtKB:P07911}.
SEQUENCE 642 AA; 70178 MW; 608ACCF13A667E64 CRC64;
MGQLSSLTSV WMVVVVTSWV IIAANIDTVE ARSCSECHSN ATCMEDGMVT TCSCLVGFTG
SGFECVDLDE CAIPGAHNCS EGSSCMNTLG SYLCTCPDGF RLTPGLGCID VDECSEPGLS
RCHALATCIN NKGNYSCVCP AGYRGDGQHC ECSPGSCGPG LDCVPVGDAL VCADPCQEHR
ILDEYWRSTE YGAGYTCDVG LNGWYRFTGP GGVRLAETCV PVLHCNTAAP MWLNGTHPTR
DQGIVNRTAC AHWRGHCCLW DASIQVKACA GGYYVYNLTE TPECYLAYCT DPTSVLGTCE
ECSVEEDCKS HDGMWSCQCK QDFNVTDLFL LDRLECRPND IKVSLSKCQL KSLGFEKVFM
YLRDSQCSGF NERGDRDWVS VVTPARDGPC GTVMVRNETH ATYSNTLYLA DEIVIRDRNI
KINFECSYPL DMKVSLETSL QPIVSSLNIS VGGTGMFTVR MALFQTPDYT QPYQGSSVTL
TTEAFLYVGT MLDGGDLSRF ALLMTNCYAT PSSNATDPLK YFIIQDRCPR TTDSTIQVVE
NGESPQGRFS VQMFRFAGNY DLVYLHCEVY LCDIINEKCK PTCSGTRFRS GGIIDQSRVL
NLGPITRKNV QAVVSRAASS SLGFLKVCLP LLLSATLTLM FQ


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