ID A0A3Q0CQZ5_MESAU Unreviewed; 1260 AA.
AC A0A3Q0CQZ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uromodulin-like 1 {ECO:0000313|RefSeq:XP_021083117.1};
GN Name=Umodl1 {ECO:0000313|RefSeq:XP_021083117.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021083117.1};
RN [1] {ECO:0000313|RefSeq:XP_021083117.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_021083117.1; XM_021227458.1.
DR AlphaFoldDB; A0A3Q0CQZ5; -.
DR STRING; 10036.ENSMAUP00000010727; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 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; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR14002; ENDOGLIN/TGF-BETA RECEPTOR TYPE III; 1.
DR PANTHER; PTHR14002:SF22; UROMODULIN-LIKE 1; 1.
DR Pfam; PF07645; EGF_CA; 2.
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; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00217; WAP; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50024; SEA; 2.
DR PROSITE; PS51390; WAP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1260
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018338755"
FT TRANSMEM 1214..1237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..106
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 114..158
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 299..413
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 410..455
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 649..736
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 733..845
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 842..879
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 936..1179
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 483..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 137757 MW; 71AB1330D46877FC CRC64;
MSRTLRLALL ALACTVDLGQ ASGFTENGLS LLSYQLCSYP VTRKVQKLQE VQTSHTAYVH
CGGWIPWKKC PKTVYRTQYL AVEVPESRNV TDCCQGFEQL GFYCVLTLNR SQEFASRPGV
CPTAEPESSR PPCSLDTDCS GLQKCCSWSG GRHCVSPALT GTQRTLVSWY NVTVLVKMGF
EDLQREDPGF RNHTRLLYSL VSALAKNLSL QWEDCPPIRD FMAFDVTSGS FHVSWSLNSS
QNHSFHVQVY KGRELLRSTW TESRTLAVPG LEAGVLYGVR VSYQGCGANI SAALVVKTDA
RVFQVTVRIM NRNLTEQLLN CNSKEFWNFS QQLFHEVENS FPQVIFDMYR RGKLRLQIVS
LQAGSLVVTL RLTLQDPEFP VGVSMLRPML QRLSESAVFQ VDQQGTLVKD WDECAHSSEH
DCHPDARCVN LEGSYTCQCL TARDASPSRA GRVCEGDMVT PTGGELSVTT KVTAPAVSLG
VTSFGPETLT LSPSPRHPRS TPTRSEAWTP GPPSKRDSSS TARQDRDGTG QGAEVSTMDP
SLGTSHGNSS GVASSFPRAP EPTHSPPQKS TDVSLHPTGE PQETFTTDPP FVAPSPTGYV
VWHPSPLWET PPPNSTRRQN EDPGPSSFPG LPPASTPVAP GPPACVPGPI GKVTVSNVTS
TGFSLKWSAA DISSSPAFYL TLVPPRGPAV IVETRDNNVT LSGLEPGALH LVEIVTKLCG
KEGTRTQLRV RTVAQKLAGE VRIANIRYSE SLQNASSSEH RDFVQLFFRA VRDSMPATMC
QHMDAGRIRM DVINVTNGSV VVEFNLLIMA DLDVREVSAA FLTALQNTSL LEVVKGKTFI
QDYNECEMRE DDCEPGTCRN TFGSFTCICD GGGPGSHVEY SGRSCDGGPS SNIVQTPGPE
WLPTPVGTRG APVPDASSVP QDLPLRLTLT DAVGVSCEIE TVVITIQKQF LQQEAIPEAS
LYLGEPSCNV SRSNGTHVFL VAGWAECGTL VQSNMTSTVV TTTLKNDLSP EGVIHHLQIL
SPIHCAFRND LLTSSGYTPQ WGVYTIIEDL HGTGNFVTEM QLFIGDSPIP QNYSVSASDE
IKIEVGLHRQ KSSLKVVLTE CWATPSSNAR DPVTFGFINN SCPVPNTYTS VIQNGNSSKA
QFKLRIFSFV NNSIVYLHCK LRVCLENPRN TCRISCNDFR LLRSSEAEHQ MSWGPLHRSE
GEPARTKPVL GTGYIVIIAV AALTVVAGAT ALLVWHFQRM RGKYNLRIQT DDFSYQVFSQ
//
