CUZD1_RAT
ID CUZD1_RAT Reviewed; 607 AA.
AC Q9QZT0; O35360; Q5D000;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=CUB and zona pellucida-like domain-containing protein 1 {ECO:0000305};
DE Short=CUB and ZP domain-containing protein 1;
DE AltName: Full=Estrogen-regulated protein 1;
DE AltName: Full=Uterus/ovary-specific protein 44;
DE Flags: Precursor;
GN Name=Cuzd1 {ECO:0000312|RGD:619771}; Synonyms=Erg1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD55939.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAD55939.1};
RC TISSUE=Uterus {ECO:0000269|PubMed:10542259};
RX PubMed=10542259; DOI=10.1074/jbc.274.45.32215;
RA Chen D., Xu X., Zhu L.-J., Angervo M., Li Q., Bagchi M.K., Bagchi I.C.;
RT "Cloning and uterus/oviduct-specific expression of a novel estrogen-
RT regulated gene (ERG1).";
RL J. Biol. Chem. 274:32215-32224(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB71895.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAB71895.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAB71895.1};
RX PubMed=11416020; DOI=10.1210/endo.142.7.8247;
RA Huynh H., Ng C.Y., Lim K.B., Ong C.K., Ong C.S., Tran E., Nguyen T.T.T.,
RA Chan T.W.M.G.;
RT "Induction of UO-44 gene expression by tamoxifen in the rat uterus and
RT ovary.";
RL Endocrinology 142:2985-2995(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-607.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Localized to zymogen granules, where it functions in
CC trypsinogen activation (By similarity). May indirectly regulate cell
CC motility, cell-cell and cell/extracellular matrix interactions (By
CC similarity). {ECO:0000250|UniProtKB:P70412,
CC ECO:0000250|UniProtKB:Q86UP6}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P70412}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P70412}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in epithelium of uterus and
CC oviduct. {ECO:0000269|PubMed:10542259, ECO:0000269|PubMed:11416020}.
CC -!- DEVELOPMENTAL STAGE: In uterus, strongly expressed at proestrus,
CC declines at estrus and disappears at diestrus. In oviduct, strongly
CC expressed at both proestrus and estrus but declines significantly at
CC diestrus. In uterus, highly expressed on day 1 of pregnancy but
CC declines dramatically on day 2 and is not detected between days 3 and
CC 7. In oviduct, highly expressed on days 1 and 2 of pregnancy but
CC declines significantly on days 3 and 4. {ECO:0000269|PubMed:10542259}.
CC -!- INDUCTION: By estrogen, tamoxifen and growth hormone. Repressed by
CC progesterone and by the antiestrogen ICI 182780.
CC {ECO:0000269|PubMed:10542259, ECO:0000269|PubMed:11416020}.
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DR EMBL; AF167170; AAD55939.1; -; mRNA.
DR EMBL; AF022147; AAB71895.1; -; mRNA.
DR EMBL; BC090345; AAH90345.1; -; mRNA.
DR RefSeq; NP_446457.1; NM_054005.1.
DR AlphaFoldDB; Q9QZT0; -.
DR SMR; Q9QZT0; -.
DR STRING; 10116.ENSRNOP00000045430; -.
DR GlyGen; Q9QZT0; 4 sites.
DR PhosphoSitePlus; Q9QZT0; -.
DR PaxDb; Q9QZT0; -.
DR GeneID; 117179; -.
DR KEGG; rno:117179; -.
DR UCSC; RGD:619771; rat.
DR CTD; 50624; -.
DR RGD; 619771; Cuzd1.
DR eggNOG; ENOG502RSDM; Eukaryota.
DR InParanoid; Q9QZT0; -.
DR OrthoDB; 776870at2759; -.
DR PhylomeDB; Q9QZT0; -.
DR PRO; PR:Q9QZT0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0042588; C:zymogen granule; ISO:RGD.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; TAS:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
DR GO; GO:0032023; P:trypsinogen activation; ISS:UniProtKB.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..607
FT /note="CUB and zona pellucida-like domain-containing
FT protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000233333"
FT TOPO_DOM 20..568
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..146
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 154..265
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 276..519
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 85..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 154..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 207..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 442..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CONFLICT 35
FT /note="S -> M (in Ref. 1; AAD55939)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="H -> T (in Ref. 3; AAH90345)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="E -> K (in Ref. 3; AAH90345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68640 MW; 68B59BCD31322012 CRC64;
MEVTGRLFIW AILAVSCRAQ LNSTAAEGRP RCTASLGGAN LGETHKALIL NLNADENCTW
TIERPENRSI RIIFSHIQLD PDSRCENESI KVFDGRSTSG PLLGEACSKN DFVPVFESSA
NSLTFQIVTD WTRVQRSVFI FYYFFSSGTT IPNCGGYLQT LEGSFSSPNY PRPHPELAYC
VWHIQVEKGY KINLNFTELF LEMDEYCRFD FIAVYDGPST TSGLLKQVCG RGTPTFESSS
DAMTVVLSTD YANSYRGFFA SYASTYVQEV NTHSLSCASD KMRVIISKSY LQSLNYHESN
LQLNDPTCRP SVSNVVEFSI PLHECGTIKK IEDHTISYTN IITFTQSPES AVITRKRHLQ
IVVTCEMEYN STVEILYITE DDVIQNQSVL GKYNTSMALY ESGSFENLIQ ESPYYVDLNQ
TLFVQATLHT SDPSLVVFLD TCRASPTSDF ASPTYDLISS GCSRDETCEV YPLFGHYGRF
QFNAFKFLRH LSSVYLKCKI LICDTSDHTS RCNQGCVSRR KRDIPSYKWK TDSVIGPIRL
KRDRLVNGDS GLLPQTHEAE ISKQPLSHLH LFSFMVLALN VVIVVTATVR HFLNRWKDHG
YQKLQVY
