CD177_MOUSE
ID CD177_MOUSE Reviewed; 817 AA.
AC Q8R2S8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=CD177 antigen;
DE AltName: CD_antigen=CD177;
DE Flags: Precursor;
GN Name=Cd177;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25359465; DOI=10.1007/s13238-014-0109-1;
RA Xie Q., Klesney-Tait J., Keck K., Parlet C., Borcherding N., Kolb R.,
RA Li W., Tygrett L., Waldschmidt T., Olivier A., Chen S., Liu G.H., Li X.,
RA Zhang W.;
RT "Characterization of a novel mouse model with genetic deletion of CD177.";
RL Protein Cell 6:117-126(2015).
CC -!- FUNCTION: In association with beta-2 integrin heterodimer ITGAM/CD11b
CC and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils
CC including degranulation and superoxide production (By similarity). In
CC addition, by preventing beta-2 integrin internalization and attenuating
CC chemokine signaling favors adhesion over migration (By similarity).
CC Heterophilic interaction with PECAM1 on endothelial cells plays a role
CC in neutrophil transendothelial migration in vitro (By similarity).
CC However, appears to be dispensable for neutrophil recruitment caused by
CC bacterial infection in vivo (PubMed:25359465). Acts as a receptor for
CC the mature form of protease PRTN3 allowing its display at the cell
CC surface of neutrophils (By similarity). By displaying PRTN3 at the
CC neutrophil cell surface, may play a role in enhancing endothelial cell
CC junctional integrity and thus vascular integrity during neutrophil
CC diapedesis (By similarity). {ECO:0000250|UniProtKB:Q8N6Q3,
CC ECO:0000269|PubMed:25359465}.
CC -!- SUBUNIT: Found in a complex with integrin ITGAM/CD11b and ITGB2/CD18.
CC Interacts with PECAM1 (via Ig-like C2-type domain 6); the interaction
CC is Ca(2+)-dependent; the interaction is direct. Interacts with serine
CC protease PRTN3/myeloblastin; the interaction tethers PRTN3 to the cell
CC surface; the interaction is direct. {ECO:0000250|UniProtKB:Q8N6Q3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25359465};
CC Single-pass type IV membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils.
CC {ECO:0000269|PubMed:25359465}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and are born at the
CC expected Mendelian rate. Slight decrease in blood CD11b(+)Ly-6G(-)Ly-
CC 6C(+) monocyte and CD11b(+)Ly-6G(+)Ly-6C(+) neutrophil populations.
CC Lymphocyte and myeloid development is not affected. In S.aureus-
CC mediated skin infection, recruitment of neutrophils and monocytes to
CC the infection site is transiently reduced. In thioglycolate-induced
CC peritonitis, recruitment of neutrophils is normal.
CC {ECO:0000269|PubMed:25359465}.
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DR EMBL; CH466593; EDL24318.1; -; Genomic_DNA.
DR EMBL; BC027283; AAH27283.1; -; mRNA.
DR CCDS; CCDS20962.1; -.
DR RefSeq; NP_081138.2; NM_026862.3.
DR AlphaFoldDB; Q8R2S8; -.
DR SMR; Q8R2S8; -.
DR STRING; 10090.ENSMUSP00000064934; -.
DR GlyGen; Q8R2S8; 4 sites.
DR PhosphoSitePlus; Q8R2S8; -.
DR MaxQB; Q8R2S8; -.
DR PaxDb; Q8R2S8; -.
DR PRIDE; Q8R2S8; -.
DR ProteomicsDB; 265620; -.
DR Antibodypedia; 65021; 420 antibodies from 24 providers.
DR DNASU; 68891; -.
DR Ensembl; ENSMUST00000063956; ENSMUSP00000064934; ENSMUSG00000052212.
DR GeneID; 68891; -.
DR KEGG; mmu:68891; -.
DR UCSC; uc009fql.1; mouse.
DR CTD; 57126; -.
DR MGI; MGI:1916141; Cd177.
DR VEuPathDB; HostDB:ENSMUSG00000052212; -.
DR eggNOG; ENOG502ST5V; Eukaryota.
DR GeneTree; ENSGT00530000063351; -.
DR HOGENOM; CLU_345789_0_0_1; -.
DR InParanoid; Q8R2S8; -.
DR OMA; CPAGYTH; -.
DR OrthoDB; 323284at2759; -.
DR PhylomeDB; Q8R2S8; -.
DR TreeFam; TF337286; -.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 68891; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cd177; mouse.
DR PRO; PR:Q8R2S8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R2S8; protein.
DR Bgee; ENSMUSG00000052212; Expressed in granulocyte and 49 other tissues.
DR Genevisible; Q8R2S8; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0070821; C:tertiary granule membrane; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0072672; P:neutrophil extravasation; ISO:MGI.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; ISO:MGI.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 5.
DR SUPFAM; SSF57302; SSF57302; 3.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..817
FT /note="CD177 antigen"
FT /id="PRO_0000378449"
FT TOPO_DOM 22..796
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 797..817
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 134..203
FT /note="UPAR/Ly6 1"
FT DOMAIN 322..393
FT /note="UPAR/Ly6 2"
FT DOMAIN 511..581
FT /note="UPAR/Ly6 3"
FT DOMAIN 705..774
FT /note="UPAR/Ly6 4"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 817 AA; 87091 MW; F22A8B073D6F7C60 CRC64;
MNSIPVLTLL GVTALLPCVP ALTCQKSSAQ AVRNVAELPL RWWGAGEKTC EVSEGCQDLI
MLLYNGPKVN LVIIKGCTEV EDQEPKVIWL RTGPGLSVVS YTRVCRHGDL CNDVNSTKIL
EELPTPTVPG SLRCPLCLSN DSCENAPEQV CPVGSTHCYD GVLRLRGDGI RTNLKVQGCM
AQPDCNLLNG TQAIGTLYMS ENCDLIGPQA LDCNSGSLET VRNVSDLHLS WTTGWQTCEA
GEGCYETVML IQNGHEFHMV LTKGCTRDMN KKARLTRHRT GPGISIVSYV HVCRDRDFCN
DLSTTDPLWT PPPDTELGTL RCRHCLSTGS CVSASELVCP AGSTHCYSGV LSLRGGGVIS
DLKVQGCISQ SQPGCNLLNG TQTIGPVDVR EDCGLQLDAL KCQHGTLKTI QDISKLPLQW
TAGQKICNVG EGCQDTLMLI ENGEQVNLVL TKGCTTAKDQ EAKVTEHRTG PGLSVTSYTR
VCRKKDFCND LSTTAPLWAP PPVTAPGTTR CPLCFSEQAC ENAPEQVCPA GSTHCYSGVL
SLRGGGIISD LKVQGCMSQP GCNLLNGTQT IGPVDVSERC SPPSETTELS CYRGVMFELG
NGFAEEPVKW TAPGSQVCAP DEICQETLLL IDVGQKSAFL GSKGCSSPGA QDNIGVSIFS
RLPGMLVASY TKFCSSHLCN GADSSSVLLS ILPRPDVPPP GDVQCPMCVE LFGSCKSTDS
VTCPRGATHC YKGDIALQGG GLTTRVSIQG CMAPPIKPLL GDSKTIGIFS AEESSNYRHE
DDVTSAPSLA WTLRLSAWML GLSALLSSLY AGICPLC
