CIROP_MOUSE
ID CIROP_MOUSE Reviewed; 699 AA.
AC A0A286YEC0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Ciliated left-right organizer metallopeptidase;
DE AltName: Full=Leishmanolysin-like peptidase 2;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9VH19};
DE Flags: Precursor;
GN Name=Cirop; Synonyms=Gm29776 {ECO:0000312|MGI:MGI:5588935};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=34903892; DOI=10.1038/s41588-021-00970-4;
RA Szenker-Ravi E., Ott T., Khatoo M., de Bellaing A.M., Goh W.X., Chong Y.L.,
RA Beckers A., Kannesan D., Louvel G., Anujan P., Ravi V., Bonnard C.,
RA Moutton S., Schoen P., Fradin M., Colin E., Megarbane A., Daou L.,
RA Chehab G., Di Filippo S., Rooryck C., Deleuze J.F., Boland A., Arribard N.,
RA Eker R., Tohari S., Ng A.Y., Rio M., Lim C.T., Eisenhaber B.,
RA Eisenhaber F., Venkatesh B., Amiel J., Crollius H.R., Gordon C.T.,
RA Gossler A., Roy S., Attie-Bitach T., Blum M., Bouvagnet P., Reversade B.;
RT "Discovery of a genetic module essential for assigning left-right asymmetry
RT in humans and ancestral vertebrates.";
RL Nat. Genet. 54:62-72(2022).
CC -!- FUNCTION: Putative metalloproteinase that plays a role in left-right
CC patterning process. {ECO:0000250|UniProtKB:A0A1D5NSK0}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08148};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08148};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in ciliated left-right
CC organizer. {ECO:0000269|PubMed:34903892}.
CC -!- DEVELOPMENTAL STAGE: Strong levels in the ventral node from the early
CC bud to the four-somite stage. Expression is enriched in the perinodal
CC crown cells and become asymmetric at the three-somite stage.
CC {ECO:0000269|PubMed:34903892}.
CC -!- SIMILARITY: Belongs to the peptidase M8 family. {ECO:0000305}.
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DR EMBL; CT009512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; A0A286YEC0; -.
DR Ensembl; ENSMUST00000224691.3; ENSMUSP00000153646.2; ENSMUSG00000114865.3.
DR MGI; MGI:5588935; Gm29776.
DR VEuPathDB; HostDB:ENSMUSG00000114865; -.
DR GeneTree; ENSGT00940000163573; -.
DR OMA; PDTPNYH; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; A0A286YEC0; protein.
DR Bgee; ENSMUSG00000114865; Expressed in granulocyte and 8 other tissues.
DR ExpressionAtlas; A0A286YEC0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0061966; P:establishment of left/right asymmetry; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR10942; PTHR10942; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|RuleBase:RU366077"
FT CHAIN 19..699
FT /note="Ciliated left-right organizer metallopeptidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5023972612"
FT TOPO_DOM 19..663
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 699 AA; 76711 MW; 03A831F8A9F29D58 CRC64;
MKMWRLLLLG VATGRCLHEE TQKSVRLLRP PFSQMPTHFR SSILPLPGSH EPRPLRIQTY
YSRAPVPGEA WDPEGETRAL AAVTETTRRI QGILAVLPVQ GPLLLSRDPA QYCHAVWGDP
DTPNYQRCSI LNPGYKGESC LGAKIPDAHL RGYSLWPEHG LPQLIQPDGP GVQNADFLLY
VQVAHTSKCH KEPSVIAYAA CCQLDSEDRP LAGTIVYCGQ HLRSPTLSHD DIVMATLHEL
LHALGFSGQL FKMWRDCPSG LSARENCSTR KQVTRRDERG QLLLTTPAVS HSLAKHLGVP
GTLQGAPLEE KQGSLSSHWE SRLLQGSIMT ATFHGAQHTR LDPVTLAAFE DSGWYQVNHS
AAEELLWGQG SGPDFGLVST CRTGSSDFFC TGSGLGCHYL HLDKGSCDSD STLEGCRIYK
PLAKGSECWK EENGLHTRAE NPHGEIYHRH SRCFLANLTS QVLSKHTSQP STAPDLEDPT
GCCYLHQCTH KGAYEVQVEG SPWIPCLPGK AVQIPGYDGL LYCPQGRLCL RDEGARAATS
QPMSFTTQDL LSQLSLRLTG TPGHSLGKGQ REELAEVVLQ ALVMRAGTSR CYFHSPTITT
SLVFTVSMWK SPGCHGPSVA MLHRTLTLTL QMKPLQVHHG EAIFTTDYSK LWTSLDHNPS
MTELLLSTGF CLLVLILVGA LGTLAYQKRA MLQVAPSTT
