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Database: UniProt
Entry: Q5R5C1
LinkDB: Q5R5C1
Original site: Q5R5C1 
ID   UROM_PONAB              Reviewed;         641 AA.
AC   Q5R5C1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 83.
DE   RecName: Full=Uromodulin;
DE   Contains:
DE     RecName: Full=Uromodulin, secreted form;
DE   Flags: Precursor;
GN   Name=UMOD;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CR860941; CAH93045.1; -; mRNA.
DR   RefSeq; NP_001126801.1; NM_001133329.1.
DR   ProteinModelPortal; Q5R5C1; -.
DR   SMR; Q5R5C1; -.
DR   STRING; 9601.ENSPPYP00000008090; -.
DR   PRIDE; Q5R5C1; -.
DR   Ensembl; ENSPPYT00000008425; ENSPPYP00000008090; ENSPPYG00000007156.
DR   GeneID; 100173805; -.
DR   KEGG; pon:100173805; -.
DR   CTD; 7369; -.
DR   eggNOG; ENOG410IVSV; Eukaryota.
DR   eggNOG; ENOG410YDU6; LUCA.
DR   GeneTree; ENSGT00940000156742; -.
DR   HOVERGEN; HBG004349; -.
DR   InParanoid; Q5R5C1; -.
DR   KO; K18274; -.
DR   OMA; GPCGTVM; -.
DR   OrthoDB; 665331at2759; -.
DR   TreeFam; TF330284; -.
DR   Proteomes; UP000001595; Chromosome 16.
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   GO; GO:0019864; F:IgG binding; IEA:Ensembl.
DR   GO; GO:0007588; P:excretion; IEA:Ensembl.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR   GO; GO:0050801; P:ion homeostasis; IEA:Ensembl.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0072218; P:metanephric ascending thin limb development; IEA:Ensembl.
DR   GO; GO:0072221; P:metanephric distal convoluted tubule development; IEA:Ensembl.
DR   GO; GO:0072233; P:metanephric thick ascending limb development; IEA:Ensembl.
DR   GO; GO:1990266; P:neutrophil migration; IEA:Ensembl.
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; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 1.
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   Calcium; Cell membrane; Cell projection; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250|UniProtKB:P07911}.
FT   CHAIN        25    614       Uromodulin.
FT                                /FTId=PRO_0000228125.
FT   CHAIN        25    587       Uromodulin, secreted form.
FT                                /FTId=PRO_0000407911.
FT   PROPEP      615    641       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000228126.
FT   DOMAIN       28     64       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       65    107       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      108    149       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      334    589       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   REGION      430    453       Important for secretion and
FT                                polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      586    589       Essential for cleavage by HPN.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   REGION      598    607       Regulates polymerization into filaments.
FT                                {ECO:0000250|UniProtKB:P07911}.
FT   SITE        587    588       Cleavage. {ECO:0000250|UniProtKB:P07911}.
FT   LIPID       614    614       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    275    275       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    322    322       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    447    447       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     32     41       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     35     50       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     52     63       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     69     83       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     77     92       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     94    106       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    112    126       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    120    135       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    137    148       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    297    306       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    300    315       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    317    347       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    335    425       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    366    389       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    506    566       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    527    582       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    571    578       {ECO:0000250|UniProtKB:P07911}.
SQ   SEQUENCE   641 AA;  69806 MW;  81AE37CB04FFDA0E CRC64;
     MGQPPLTWML MVVVASWFIT TAATNTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG
     LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC
     HALATCVNVV GNYLCVCPAG YRGDGWHCEC SPGSCGPGLD CVPEGDALVC ADPCQAHRTL
     DEYWRSTEYG EGYACDTDLR GWYRFVGQGG ARLAETCVPV LRCNTAAPMW LNGTHPSSDE
     GIVSRKACAH WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC
     SIDEDCKSDN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK SLGFDKVFMY
     LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA TYSNTLYLAD EIIIRDRNIK
     INFACSYPLD MKVSLKTSLQ PVVSALNITV GGTGMFTVRM ALFQNPSYTQ PYQGSSVTLS
     TEAFLYVGTM LDGGDLSRFA LLMTNCYATP SGNATDPLKY FIIQDRCPHT RDSTIQVVEN
     GESSQGRFSV QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN
     LGPITRKGVQ ATVSRAAFSS LGLLKVWLPL LLSATLTLTF Q
//
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