UROL1_MOUSE
ID UROL1_MOUSE Reviewed; 1319 AA.
AC Q5DID3; Q5DID1; Q5DID2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Uromodulin-like 1;
DE AltName: Full=Olfactorin;
DE Flags: Precursor;
GN Name=Umodl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION,
RP TOPOLOGY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=16026467; DOI=10.1111/j.1460-9568.2005.04164.x;
RA Di Schiavi E., Riano E., Heye B., Bazzicalupo P., Rugarli E.I.;
RT "UMODL1/olfactorin is an extracellular membrane-bound molecule with a
RT restricted spatial expression in olfactory and vomeronasal neurons.";
RL Eur. J. Neurosci. 21:3291-3300(2005).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=15682396; DOI=10.1002/cne.20429;
RA Yu T.-T., McIntyre J.C., Bose S.C., Hardin D., Owen M.C., McClintock T.S.;
RT "Differentially expressed transcripts from phenotypically identified
RT olfactory sensory neurons.";
RL J. Comp. Neurol. 483:251-262(2005).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16026467};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16026467}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5DID3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DID3-2; Sequence=VSP_017661;
CC Name=3;
CC IsoId=Q5DID3-3; Sequence=VSP_017660;
CC -!- DEVELOPMENTAL STAGE: First detected at 16.5 dpc only in olfactory
CC epithelium (OE) and the epithelium of the vomeronasal organ (VNO). At
CC this stage, expression in OE is punctate and is restricted to only some
CC of the sensory neurons. At birth and postnatally, expression in these
CC organs extends to more neurons. At 3 weeks, expression shows a smooth
CC gradation from high apical to low basal within the layer of mature
CC olfactory sensory neurons of the olfactory epithelium.
CC {ECO:0000269|PubMed:15682396, ECO:0000269|PubMed:16026467}.
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DR EMBL; AY771616; AAX14811.1; -; mRNA.
DR EMBL; AY771617; AAX14812.1; -; mRNA.
DR EMBL; AY771618; AAX14813.1; -; mRNA.
DR CCDS; CCDS37543.1; -. [Q5DID3-2]
DR RefSeq; NP_803416.2; NM_177465.4. [Q5DID3-2]
DR RefSeq; XP_006524677.1; XM_006524614.2. [Q5DID3-1]
DR AlphaFoldDB; Q5DID3; -.
DR SMR; Q5DID3; -.
DR BioGRID; 206331; 2.
DR STRING; 10090.ENSMUSP00000110202; -.
DR GlyGen; Q5DID3; 9 sites.
DR iPTMnet; Q5DID3; -.
DR PhosphoSitePlus; Q5DID3; -.
DR PaxDb; Q5DID3; -.
DR PRIDE; Q5DID3; -.
DR ProteomicsDB; 275391; -. [Q5DID3-1]
DR ProteomicsDB; 275392; -. [Q5DID3-2]
DR ProteomicsDB; 275393; -. [Q5DID3-3]
DR Antibodypedia; 42290; 46 antibodies from 11 providers.
DR DNASU; 52020; -.
DR Ensembl; ENSMUST00000066554; ENSMUSP00000067443; ENSMUSG00000054134. [Q5DID3-2]
DR Ensembl; ENSMUST00000066981; ENSMUSP00000065470; ENSMUSG00000054134. [Q5DID3-3]
DR Ensembl; ENSMUST00000114555; ENSMUSP00000110202; ENSMUSG00000054134. [Q5DID3-2]
DR Ensembl; ENSMUST00000235156; ENSMUSP00000157913; ENSMUSG00000054134. [Q5DID3-3]
DR Ensembl; ENSMUST00000237889; ENSMUSP00000157726; ENSMUSG00000054134. [Q5DID3-1]
DR GeneID; 52020; -.
DR KEGG; mmu:52020; -.
DR UCSC; uc008buf.1; mouse. [Q5DID3-2]
DR UCSC; uc008bug.1; mouse. [Q5DID3-1]
DR UCSC; uc008buh.1; mouse. [Q5DID3-3]
DR CTD; 89766; -.
DR MGI; MGI:1929785; Umodl1.
DR VEuPathDB; HostDB:ENSMUSG00000054134; -.
DR eggNOG; ENOG502QVDQ; Eukaryota.
DR GeneTree; ENSGT00940000159975; -.
DR HOGENOM; CLU_005456_0_0_1; -.
DR InParanoid; Q5DID3; -.
DR OMA; QEHDCEP; -.
DR OrthoDB; 131214at2759; -.
DR PhylomeDB; Q5DID3; -.
DR TreeFam; TF329882; -.
DR BioGRID-ORCS; 52020; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q5DID3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5DID3; protein.
DR Bgee; ENSMUSG00000054134; Expressed in olfactory epithelium and 32 other tissues.
DR ExpressionAtlas; Q5DID3; baseline and differential.
DR Genevisible; Q5DID3; MM.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0060612; P:adipose tissue development; IDA:MGI.
DR GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IDA:MGI.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IDA:MGI.
DR GO; GO:1990266; P:neutrophil migration; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
DR GO; GO:0050793; P:regulation of developmental process; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:1904708; P:regulation of granulosa cell apoptotic process; IDA:MGI.
DR GO; GO:2000354; P:regulation of ovarian follicle development; IDA:MGI.
DR GO; GO:2000241; P:regulation of reproductive process; IDA:MGI.
DR GO; GO:0007338; P:single fertilization; IDA:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.4100; -; 1.
DR Gene3D; 4.10.75.10; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR008197; WAP_dom.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00095; WAP; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00217; WAP; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50024; SEA; 2.
DR PROSITE; PS51390; WAP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1319
FT /note="Uromodulin-like 1"
FT /id="PRO_0000228128"
FT TOPO_DOM 23..1273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1295..1319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..107
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 115..159
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 265..306
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 307..391
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 389..503
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 500..545
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 709..795
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 792..904
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 901..945
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 995..1238
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 569..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..95
FT /evidence="ECO:0000255"
FT DISULFID 62..71
FT /evidence="ECO:0000255"
FT DISULFID 94..105
FT /evidence="ECO:0000255"
FT DISULFID 269..283
FT /evidence="ECO:0000250"
FT DISULFID 277..292
FT /evidence="ECO:0000250"
FT DISULFID 504..518
FT /evidence="ECO:0000250"
FT DISULFID 512..527
FT /evidence="ECO:0000250"
FT DISULFID 529..544
FT /evidence="ECO:0000250"
FT DISULFID 905..917
FT /evidence="ECO:0000250"
FT DISULFID 912..926
FT /evidence="ECO:0000250"
FT DISULFID 928..944
FT /evidence="ECO:0000250"
FT DISULFID 1160..1218
FT /evidence="ECO:0000250"
FT VAR_SEQ 622
FT /note="G -> GMEVPNVTPNLGKTHRSTSGVTSSVPWAPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16026467"
FT /id="VSP_017661"
FT VAR_SEQ 707..792
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16026467"
FT /id="VSP_017660"
SQ SEQUENCE 1319 AA; 145320 MW; AAD4206B95B4270E CRC64;
MMSRTVRLVL LALACTVDLS QASGFTENGL SLLSYQLCSY PVTRSVQKLQ AVQTSHTAYV
YCGGWIPWKK CPKTVYRTQY LAMDVPESRN VTDCCAGFEQ LGLYCVLSLN RSREFASRPG
VCPTAEAEPL SPSCSLDTDC SGLQKCCSWP GGRHCVSPTP TGTEKSMVSW YNVTVLVKVG
FEDLQREDPG LRNHTRLLYS LVTSALQPLN PAVHYLTSTG GKDTFTTVSW LLMGFPRLMT
VANVSVMLDD MVNRVYEVVS IQVQDVNECL HSELQACSVR EQCRNLEGSY QCVSSQRLNH
TDEDCPPIRD FVALNVTSSS FHVSWSLNST QNYNFHIQVY KGKEILRSAW TRGHTMAVSD
LEAGVLYRVR TSYLGCGANV SATLVVKTDA QVFQVTIRIM DRNLTEQILD CSSGEFWNFS
RQLFHEVQNS FPQAISDLYR QGRLRMQIVS LQAGSLVVTL RLTLQDPDFS VGVHTLTPML
PVLSVSNVFQ VDQQRTFVQD WDECAHSSEH DCHPSARCIN LEGSYTCQCL TARDASPSRA
GRVCEGDMVI PTGDELSVTT KVTVPAASTG ITTFGPETLT ESLSSKHPRS TPARSQTWTP
VPPSVRDGGS IVRQDRNSTG QGQTHGTHQG TTDAPLHTTR ESQELITKDP PFLTATTTGY
VVWHSSPTWK TPPNSTRLQN EDPRSSSFPG PPSAPTDVTP ESPACVPGPI GKVTVSNVTS
TSFSLEWPAD IRLSPAFHLT LVSPRGPAMT METQNNNVTL SGLEWGTLYL VEIVAKVCGK
EGARTQLKVR TVAQKLAGNV RITSMQYSES FLNTSSREHR EFVELFFRTV RDSLPATLRQ
HMDAGRIRVD IINITNGSIV VEFNLLMTAD LDVREVSAGF LNALQNTSML EVVRGKTFMQ
DYNECDMKED DCAPGTCRNT FGSFTCSCDE GGPDSQVEYS GRSCDGDPSG NMTQTPGSEW
SPTPAGTRGV PVPIASSTAQ DLPLRLNLMD AVSVSCEIET VIITIQKRFL QQAAIPEASL
YLGEPSCNVS RSNSTHVFLV AGWGECGTIL QSNMTTTVVT TTLRNNLSPE GVIHHPQFLS
PIHCAFQNDV LTSSGYTPQW GVYTVIEDLH GTGNFVTEMQ LYIGDSPIPQ NYSVSASDEI
KIEVGLHRQK SSLKVVLTEC WATPSSNAKD PVTFSFINNS CPVPNTYTSV IQNGHSSKAQ
FKLRIFSFIN NSIVYLHCKL RVCMENPRNS CRISCNDFRS LRSSEALHQM TWGPLHRTEG
AQACTKPVLG TGYIILLAAA ALLVVAGATT LLILRYQRVR QKYNLRIQTD DFSYQVFSQ
