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Database: UniProt
Entry: Q862Z3
LinkDB: Q862Z3
Original site: Q862Z3 
ID   UROM_CANLF              Reviewed;         642 AA.
AC   Q862Z3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-APR-2019, entry version 101.
DE   RecName: Full=Uromodulin;
DE   AltName: Full=Tamm-Horsfall urinary glycoprotein;
DE            Short=THP;
DE   Contains:
DE     RecName: Full=Uromodulin, secreted form;
DE   Flags: Precursor;
GN   Name=UMOD;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12751332; DOI=10.1080/1042517021000056943;
RA   Cox M.L., Quignon P., Galibert F., Lees G.E., Murphy K.E.;
RT   "Sequencing and radiation hybrid mapping of canine uromodulin.";
RL   DNA Seq. 14:61-69(2003).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=1531535; DOI=10.1073/pnas.89.4.1189;
RA   Fukuoka S., Freedman S.D., Yu H., Sukhatme V.P., Scheele G.A.;
RT   "GP-2/THP gene family encodes self-binding
RT   glycosylphosphatidylinositol-anchored proteins in apical secretory
RT   compartments of pancreas and kidney.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1189-1193(1992).
CC   -!- FUNCTION: Uromodulin: Functions in biogenesis and organization of
CC       the apical membrane of epithelial cells of the thick ascending
CC       limb of Henle's loop (TALH), where it promotes formation of
CC       complex filamentous gel-like structure that may play a role in the
CC       water barrier permeability. May serve as a receptor for binding
CC       and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates
CC       neutrophil migration across renal epithelia.
CC       {ECO:0000250|UniProtKB:P07911}.
CC   -!- FUNCTION: Uromodulin, secreted form: In the urine, may contribute
CC       to colloid osmotic pressure, retards passage of positively charged
CC       electrolytes, prevents urinary tract infection and inhibits
CC       formation of liquid containing supersaturated salts and subsequent
CC       formation of salt crystals. {ECO:0000250|UniProtKB:Q91X17}.
CC   -!- SUBUNIT: Uromodulin, secreted form: homodimer that then
CC       polymerizes into long filaments. {ECO:0000250|UniProtKB:P07911}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:P07911}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P07911}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:P07911}. Cell projection, cilium membrane
CC       {ECO:0000250|UniProtKB:P07911}. Note=Only a small fraction sorts
CC       to the basolateral pole of tubular epithelial cells compared to
CC       apical localization. Secreted into urine after cleavage.
CC       Colocalizes with NPHP1 and KIF3A. {ECO:0000250|UniProtKB:P07911}.
CC   -!- SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted
CC       {ECO:0000250|UniProtKB:P07911}. Note=Detected in urine.
CC       {ECO:0000250|UniProtKB:P07911}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney and pancreas.
CC       {ECO:0000269|PubMed:1531535}.
CC   -!- DOMAIN: The ZP domain mediates polymerization, leading to the
CC       formation of long filaments. {ECO:0000250|UniProtKB:P07911}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07911}.
CC   -!- PTM: Proteolytically cleaved at a conserved C-terminal proteolytic
CC       cleavage site to generate the secreted form found in urine. This
CC       cleavage is catalyzed by HPN. {ECO:0000250|UniProtKB:P07911}.
DR   EMBL; AF498324; AAO33163.1; -; mRNA.
DR   UniGene; Cfa.4; -.
DR   ProteinModelPortal; Q862Z3; -.
DR   SMR; Q862Z3; -.
DR   STRING; 9612.ENSCAFP00000026625; -.
DR   PaxDb; Q862Z3; -.
DR   eggNOG; ENOG410IVSV; Eukaryota.
DR   eggNOG; ENOG410YDU6; LUCA.
DR   HOGENOM; HOG000293303; -.
DR   HOVERGEN; HBG004349; -.
DR   InParanoid; Q862Z3; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   PRINTS; PR00023; ZPELLUCIDA.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     26       {ECO:0000250|UniProtKB:P07911}.
FT   CHAIN        27    620       Uromodulin.
FT                                /FTId=PRO_0000041669.
FT   CHAIN        27    588       Uromodulin, secreted form.
FT                                /FTId=PRO_0000407908.
FT   PROPEP      621    642       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000041670.
FT   DOMAIN       32     64       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       67    109       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      110    151       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      335    590       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   REGION      431    454       Important for secretion and
FT                                polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      587    590       Essential for cleavage by HPN.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      599    608       Regulates polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   SITE        588    589       Cleavage. {ECO:0000250|UniProtKB:P07911}.
FT   LIPID       620    620       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     78     78       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    134    134       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    234    234       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    277    277       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     34     43       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     37     52       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     54     65       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     71     85       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     79     94       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     96    108       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    114    128       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    122    137       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    139    150       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    299    308       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    302    317       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    319    348       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    336    426       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    367    390       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    507    567       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    528    583       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    572    579       {ECO:0000250|UniProtKB:P07911}.
SQ   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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