CD177_HUMAN
ID CD177_HUMAN Reviewed; 437 AA.
AC Q8N6Q3; Q711Q2; Q8NCV9; Q96QH1; Q9HDA5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=CD177 antigen {ECO:0000312|HGNC:HGNC:30072};
DE AltName: Full=Human neutrophil alloantigen 2a {ECO:0000305|PubMed:11465086};
DE Short=HNA-2a {ECO:0000305|PubMed:11465086};
DE AltName: Full=NB1 glycoprotein {ECO:0000305|PubMed:11465086};
DE Short=NB1 GP {ECO:0000305|PubMed:11465086};
DE AltName: Full=Polycythemia rubra vera protein 1 {ECO:0000303|PubMed:10753836};
DE Short=PRV-1 {ECO:0000303|PubMed:10753836};
DE AltName: CD_antigen=CD177;
DE Flags: Precursor;
GN Name=CD177 {ECO:0000312|HGNC:HGNC:30072};
GN Synonyms=NB1, PRV1 {ECO:0000303|PubMed:10753836}; ORFNames=UNQ595/PRO1181;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-251, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10753836;
RA Temerinac S., Klippel S., Strunck E., Roeder S., Luebbert M., Lange W.,
RA Azemar M., Meinhardt G., Schaefer H.-E., Pahl H.L.;
RT "Cloning of PRV-1, a novel member of the uPAR receptor superfamily, which
RT is overexpressed in polycythemia rubra vera.";
RL Blood 95:2569-2576(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-45; 167-175
RP AND 386-393, VARIANTS PRO-3; PHE-119; ILE-251; GLN-323 AND SER-379, MASS
RP SPECTROMETRY, AND GLYCOSYLATION.
RX PubMed=11465086;
RX DOI=10.1002/1521-4141(200105)31:5<1301::aid-immu1301>3.0.co;2-j;
RA Kissel K., Santoso S., Hofmann C., Stroncek D., Bux J.;
RT "Molecular basis of the neutrophil glycoprotein NB1 (CD177) involved in the
RT pathogenesis of immunenneutropenia and transfusion reactions.";
RL Eur. J. Immunol. 31:1301-1309(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND VARIANT PRO-3.
RX PubMed=12010833; DOI=10.1182/blood.v99.11.4231;
RA Kissel K., Scheffler S., Kerowgan M., Bux J.;
RT "Molecular basis of NB1 (HNA-2a, CD177) deficiency.";
RL Blood 99:4231-4233(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-251.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-251.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-3 AND
RP THR-348.
RC TISSUE=Colon;
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 [7]
RP PROTEIN SEQUENCE OF 22-36.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND SHEDDING.
RX PubMed=12239154; DOI=10.1182/blood-2002-03-0949;
RA Klippel S., Strunck E., Busse C.E., Behringer D., Pahl H.L.;
RT "Biochemical characterization of PRV-1, a novel hematopoietic cell surface
RT receptor, which is overexpressed in polycythemia rubra vera.";
RL Blood 100:2441-2448(2002).
RN [9]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12377969; DOI=10.1200/jco.2002.11.507;
RA Teofili L., Martini M., Luongo M., Di Mario A., Leone G., De Stefano V.,
RA Larocca L.M.;
RT "Overexpression of the polycythemia rubra vera-1 gene in essential
RT thrombocythemia.";
RL J. Clin. Oncol. 20:4249-4254(2002).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12675722; DOI=10.1046/j.1537-2995.2003.00320.x;
RA Caruccio L., Bettinotti M., Matsuo K., Sharon V., Stroncek D.;
RT "Expression of human neutrophil antigen-2a (NB1) is increased in
RT pregnancy.";
RL Transfusion 43:357-363(2003).
RN [11]
RP FUNCTION, INTERACTION WITH PRTN3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=17244676; DOI=10.1182/blood-2006-10-055327;
RA von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M.,
RA Cristina Cardoso M., Luft F.C., Kettritz R.;
RT "NB1 mediates surface expression of the ANCA antigen proteinase 3 on human
RT neutrophils.";
RL Blood 109:4487-4493(2007).
RN [12]
RP FUNCTION, INTERACTION WITH PECAM1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17580308; DOI=10.1074/jbc.m701120200;
RA Sachs U.J., Andrei-Selmer C.L., Maniar A., Weiss T., Paddock C.,
RA Orlova V.V., Choi E.Y., Newman P.J., Preissner K.T., Chavakis T.,
RA Santoso S.;
RT "The neutrophil-specific antigen CD177 is a counter-receptor for platelet
RT endothelial cell adhesion molecule-1 (CD31).";
RL J. Biol. Chem. 282:23603-23612(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=18462208; DOI=10.1111/j.1365-2249.2008.03663.x;
RA von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.;
RT "Neutrophil surface presentation of the anti-neutrophil cytoplasmic
RT antibody-antigen proteinase 3 depends on N-terminal processing.";
RL Clin. Exp. Immunol. 152:508-516(2008).
RN [14]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGAM AND ITGB2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21193407; DOI=10.1074/jbc.m110.171256;
RA Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F.,
RA Kettritz R.;
RT "Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA
RT neutrophil activation.";
RL J. Biol. Chem. 286:7070-7081(2011).
RN [15]
RP FUNCTION.
RX PubMed=23202369; DOI=10.1161/atvbaha.112.300474;
RA Kuckleburg C.J., Newman P.J.;
RT "Neutrophil proteinase 3 acts on protease-activated receptor-2 to enhance
RT vascular endothelial cell barrier function.";
RL Arterioscler. Thromb. Vasc. Biol. 33:275-284(2013).
RN [16]
RP FUNCTION.
RX PubMed=23461681; DOI=10.1111/ejh.12095;
RA Wang L., Ge S., Agustian A., Hiss M., Haller H., von Vietinghoff S.;
RT "Surface receptor CD177/NB1 does not confer a recruitment advantage to
RT neutrophilic granulocytes during human peritonitis.";
RL Eur. J. Haematol. 90:436-437(2013).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24926686; DOI=10.1371/journal.pone.0099671;
RA Hu N., Mora-Jensen H., Theilgaard-Moench K., Doornbos-van der Meer B.,
RA Huitema M.G., Stegeman C.A., Heeringa P., Kallenberg C.G., Westra J.;
RT "Differential expression of granulopoiesis related genes in neutrophil
RT subsets distinguished by membrane expression of CD177.";
RL PLoS ONE 9:E99671-E99671(2014).
RN [18]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGAM AND ITGB2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28807980; DOI=10.1182/blood-2017-03-768507;
RA Bai M., Grieshaber-Bouyer R., Wang J., Schmider A.B., Wilson Z.S., Zeng L.,
RA Halyabar O., Godin M.D., Nguyen H.N., Levescot A., Cunin P., Lefort C.T.,
RA Soberman R.J., Nigrovic P.A.;
RT "CD177 modulates human neutrophil migration through activation-mediated
RT integrin and chemoreceptor regulation.";
RL Blood 130:2092-2100(2017).
RN [19]
RP INTERACTION WITH PRTN3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28240246; DOI=10.1038/srep43328;
RA Jerke U., Marino S.F., Daumke O., Kettritz R.;
RT "Characterization of the CD177 interaction with the ANCA antigen proteinase
RT 3.";
RL Sci. Rep. 7:43328-43328(2017).
RN [20]
RP VARIANT THR-348, AND POLYMORPHISM.
RX PubMed=12623849; DOI=10.1182/blood-2002-09-2831;
RA Wolff J., Brendel C., Fink L., Bohle R.M., Kissel K., Bux J.;
RT "Lack of NB1 GP (CD177/HNA-2a) gene transcription in NB1 GP-neutrophils
RT from NB1 GP-expressing individuals and association of low expression with
RT NB1 gene polymorphisms.";
RL Blood 102:731-733(2003).
RN [21]
RP VARIANTS PRO-3; PHE-119; GLN-323 AND SER-379, AND POLYMORPHISM.
RX PubMed=14692971; DOI=10.1046/j.0041-1132.2004.00606.x;
RA Caruccio L., Walkovich K., Bettinotti M., Schuller R., Stroncek D.;
RT "CD177 polymorphisms: correlation between high-frequency single nucleotide
RT polymorphisms and neutrophil surface protein expression.";
RL Transfusion 44:77-82(2004).
RN [22]
RP VARIANTS PRO-3; LEU-31; ILE-251; ALA-261; THR-348 AND ARG-431, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND POLYMORPHISM.
RX PubMed=27227454; DOI=10.1371/journal.pgen.1006067;
RA Wu Z., Liang R., Ohnesorg T., Cho V., Lam W., Abhayaratna W.P.,
RA Gatenby P.A., Perera C., Zhang Y., Whittle B., Sinclair A., Goodnow C.C.,
RA Field M., Andrews T.D., Cook M.C.;
RT "Heterogeneity of human neutrophil CD177 expression results from CD177P1
RT pseudogene conversion.";
RL PLoS Genet. 12:E1006067-E1006067(2016).
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 (PubMed:21193407). In
CC addition, by preventing beta-2 integrin internalization and attenuating
CC chemokine signaling favors adhesion over migration (PubMed:28807980).
CC Heterophilic interaction with PECAM1 on endothelial cells plays a role
CC in neutrophil transendothelial migration in vitro (PubMed:17580308).
CC However, appears to be dispensable for neutrophil recruitment caused by
CC bacterial infection in vivo (PubMed:23461681). Acts as a receptor for
CC the mature form of protease PRTN3 allowing its display at the cell
CC surface of neutrophils (PubMed:17244676, PubMed:18462208). By
CC displaying PRTN3 at the neutrophil cell surface, may play a role in
CC enhancing endothelial cell junctional integrity and thus vascular
CC integrity during neutrophil diapedesis (PubMed:23202369).
CC {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:17580308,
CC ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:21193407,
CC ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:23461681,
CC ECO:0000269|PubMed:28807980}.
CC -!- SUBUNIT: Found in a complex with integrin ITGAM/CD11b and ITGB2/CD18
CC (PubMed:28807980, PubMed:21193407). Interacts with PECAM1 (via Ig-like
CC C2-type domain 6); the interaction is Ca(2+)-dependent; the interaction
CC is direct (PubMed:17580308). Interacts with serine protease
CC PRTN3/myeloblastin; the interaction tethers PRTN3 to the cell surface;
CC the interaction is direct (PubMed:17244676, PubMed:28240246).
CC {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:17580308,
CC ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:28240246,
CC ECO:0000269|PubMed:28807980}.
CC -!- INTERACTION:
CC Q8N6Q3; Q9Y2W7: KCNIP3; NbExp=9; IntAct=EBI-747170, EBI-751501;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12239154,
CC ECO:0000269|PubMed:12675722, ECO:0000269|PubMed:17244676,
CC ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18462208,
CC ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:24926686,
CC ECO:0000269|PubMed:27227454, ECO:0000269|PubMed:28240246,
CC ECO:0000269|PubMed:28807980}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676}. Membrane
CC raft {ECO:0000269|PubMed:21193407}; Lipid-anchor, GPI-like-anchor
CC {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676}. Secreted
CC {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:18462208}. Cytoplasmic
CC granule membrane {ECO:0000269|PubMed:18462208}. Cell projection,
CC lamellipodium {ECO:0000269|PubMed:28807980}. Note=Cell surface
CC expression on neutrophils is increased upon TNF-alpha, fMLP or
CC CXCL8/IL8-mediated stimulation (PubMed:17244676, PubMed:17580308). In
CC neutrophils, stored predominantly in secondary and tertiary granules
CC (PubMed:18462208). Can also be shedded from the cell membrane
CC (PubMed:12239154, PubMed:18462208). Localizes to lamellar protrusions
CC in spreading neutrophils (PubMed:28807980).
CC {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676,
CC ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18462208,
CC ECO:0000269|PubMed:28807980}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N6Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6Q3-2; Sequence=VSP_017860, VSP_017861;
CC Name=3;
CC IsoId=Q8N6Q3-3; Sequence=VSP_017858, VSP_017859;
CC -!- TISSUE SPECIFICITY: Highly expressed in normal bone marrow and weakly
CC expressed in fetal liver (PubMed:10753836). During neutrophil
CC differentiation, expression begins at the metamyelocyte stage and
CC continues throughout the subsequent stages (at protein level)
CC (PubMed:17244676, PubMed:18462208, PubMed:24926686). Expressed by a
CC subset of mature neutrophils (at protein level) (PubMed:10753836,
CC PubMed:28240246, PubMed:12377969, PubMed:18462208, PubMed:12675722,
CC PubMed:17244676, PubMed:17580308, PubMed:21193407, PubMed:24926686,
CC PubMed:28807980, PubMed:27227454). The percentage of neutrophils
CC expressing CD177 varies across the population (PubMed:17244676,
CC PubMed:27227454). Expressed in granulocytes of patients with
CC polycythemia vera (PV) and with essential thrombocythemia (ET)
CC (PubMed:10753836, PubMed:12377969). {ECO:0000269|PubMed:10753836,
CC ECO:0000269|PubMed:12377969, ECO:0000269|PubMed:12675722,
CC ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:17580308,
CC ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:21193407,
CC ECO:0000269|PubMed:27227454, ECO:0000269|PubMed:28240246,
CC ECO:0000269|PubMed:28807980}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neonatal and adult neutrophils.
CC {ECO:0000269|PubMed:18462208}.
CC -!- INDUCTION: By CSF3/G-CSF in resting granulocytes (PubMed:10753836).
CC Induced during CSF3/G-CSF-mediated neutrophil differentiation
CC (PubMed:17244676, PubMed:18462208). Induced during pregnancy
CC (PubMed:12675722). Induced in patients with polycythemia vera (PV) and
CC with essential thrombocythemia (ET) (PubMed:10753836, PubMed:12377969).
CC {ECO:0000269|PubMed:10753836, ECO:0000269|PubMed:12377969,
CC ECO:0000269|PubMed:12675722, ECO:0000269|PubMed:17244676,
CC ECO:0000269|PubMed:18462208}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11465086,
CC ECO:0000269|PubMed:12239154}.
CC -!- PTM: A soluble form may also be produced by proteolytic cleavage at the
CC cell surface (shedding). {ECO:0000269|PubMed:12239154,
CC ECO:0000269|PubMed:18462208}.
CC -!- MASS SPECTROMETRY: Mass=50556; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11465086};
CC -!- POLYMORPHISM: There is a significant association between the variants
CC Ala-3, Leu-251 and Thr-348 and a low expression of CD177 on neutrophils
CC (PubMed:12623849, PubMed:14692971). Expression of CD177 on neutrophils
CC is a trait determined by ratio of CD177/CD177P1 alleles
CC (PubMed:27227454). The phenotype of CD177 null neutrophils is due to
CC recombination between exon 7 of CD177 and the pseudogene CD177P1
CC through gene conversion, changing Lys-263 codon into stop codon
CC (PubMed:27227454). The lack of CD177 expression affects 1-10 percent of
CC the population placing them at risk for formation of anti-neutrophil
CC antibodies that can cause transfusion-related acute lung injury and
CC neonatal alloimmune neutropenia. {ECO:0000269|PubMed:12623849,
CC ECO:0000269|PubMed:14692971, ECO:0000269|PubMed:27227454}.
CC -!- MISCELLANEOUS: [Isoform 2]: Associated with CD177-negative phenotype.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Associated with CD177-negative phenotype.
CC {ECO:0000305}.
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DR EMBL; AF146747; AAG00895.1; -; mRNA.
DR EMBL; AJ290452; CAC44459.1; -; mRNA.
DR EMBL; AJ305326; CAC83758.1; -; mRNA.
DR EMBL; AJ310433; CAC83724.1; -; mRNA.
DR EMBL; AY358932; AAQ89291.1; -; mRNA.
DR EMBL; BT020111; AAV38914.1; -; mRNA.
DR EMBL; BC029167; AAH29167.1; -; mRNA.
DR CCDS; CCDS62700.1; -. [Q8N6Q3-1]
DR RefSeq; NP_065139.2; NM_020406.3.
DR AlphaFoldDB; Q8N6Q3; -.
DR SMR; Q8N6Q3; -.
DR BioGRID; 121389; 4.
DR IntAct; Q8N6Q3; 101.
DR STRING; 9606.ENSP00000479536; -.
DR GlyGen; Q8N6Q3; 1 site.
DR PhosphoSitePlus; Q8N6Q3; -.
DR BioMuta; CD177; -.
DR DMDM; 91208246; -.
DR jPOST; Q8N6Q3; -.
DR MassIVE; Q8N6Q3; -.
DR PaxDb; Q8N6Q3; -.
DR PeptideAtlas; Q8N6Q3; -.
DR PRIDE; Q8N6Q3; -.
DR ProteomicsDB; 72212; -. [Q8N6Q3-1]
DR ProteomicsDB; 72213; -. [Q8N6Q3-2]
DR ProteomicsDB; 72214; -. [Q8N6Q3-3]
DR DNASU; 57126; -.
DR Ensembl; ENST00000378012.3; ENSP00000367251.2; ENSG00000204936.10. [Q8N6Q3-3]
DR GeneID; 57126; -.
DR KEGG; hsa:57126; -.
DR UCSC; uc060zla.1; human. [Q8N6Q3-1]
DR CTD; 57126; -.
DR DisGeNET; 57126; -.
DR GeneCards; CD177; -.
DR HGNC; HGNC:30072; CD177.
DR MIM; 162860; gene.
DR neXtProt; NX_Q8N6Q3; -.
DR OpenTargets; ENSG00000204936; -.
DR PharmGKB; PA142672147; -.
DR VEuPathDB; HostDB:ENSG00000204936; -.
DR eggNOG; ENOG502ST5V; Eukaryota.
DR GeneTree; ENSGT00530000063351; -.
DR InParanoid; Q8N6Q3; -.
DR OrthoDB; 1103796at2759; -.
DR PhylomeDB; Q8N6Q3; -.
DR PathwayCommons; Q8N6Q3; -.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8N6Q3; -.
DR BioGRID-ORCS; 57126; 21 hits in 646 CRISPR screens.
DR GeneWiki; CD177; -.
DR GenomeRNAi; 57126; -.
DR Pharos; Q8N6Q3; Tbio.
DR PRO; PR:Q8N6Q3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N6Q3; protein.
DR Bgee; ENSG00000204936; Expressed in rectum and 108 other tissues.
DR ExpressionAtlas; Q8N6Q3; baseline and differential.
DR Genevisible; Q8N6Q3; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
DR GO; GO:1990266; P:neutrophil migration; IMP:UniProtKB.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; IGI:UniProtKB.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:UniProtKB.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 2.
DR SUPFAM; SSF57302; SSF57302; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Glycoprotein; GPI-anchor; Immunity;
KW Innate immunity; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 22..408
FT /note="CD177 antigen"
FT /id="PRO_0000231643"
FT PROPEP 409..437
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000231644"
FT DOMAIN 133..210
FT /note="UPAR/Ly6 1"
FT DOMAIN 325..377
FT /note="UPAR/Ly6 2"
FT LIPID 408
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 129..145
FT /note="GSLRCPVCLSMEGCLEG -> MMGAAEGPFGKAEQVDS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:12010833"
FT /id="VSP_017858"
FT VAR_SEQ 146..437
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12010833"
FT /id="VSP_017859"
FT VAR_SEQ 210..248
FT /note="TCHRGTTIMTHGNLAQEPTDWTTSNTEMCEVGQVCQETL -> QLKPVGLLE
FT EHNVGEKERGQGQHQCVQLDWQKRAATGIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12010833"
FT /id="VSP_017860"
FT VAR_SEQ 249..437
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12010833"
FT /id="VSP_017861"
FT VARIANT 3
FT /note="A -> P (in dbSNP:rs45441892)"
FT /evidence="ECO:0000269|PubMed:11465086,
FT ECO:0000269|PubMed:12010833, ECO:0000269|PubMed:14692971,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:27227454"
FT /id="VAR_025858"
FT VARIANT 31
FT /note="H -> L (in dbSNP:rs45553433)"
FT /evidence="ECO:0000269|PubMed:27227454"
FT /id="VAR_079754"
FT VARIANT 119
FT /note="L -> F"
FT /evidence="ECO:0000269|PubMed:11465086,
FT ECO:0000269|PubMed:14692971"
FT /id="VAR_026156"
FT VARIANT 251
FT /note="L -> I (in dbSNP:rs10425835)"
FT /evidence="ECO:0000269|PubMed:10753836,
FT ECO:0000269|PubMed:11465086, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:27227454, ECO:0000269|Ref.5"
FT /id="VAR_025859"
FT VARIANT 261
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:27227454"
FT /id="VAR_079755"
FT VARIANT 323
FT /note="R -> Q"
FT /evidence="ECO:0000269|PubMed:11465086,
FT ECO:0000269|PubMed:14692971"
FT /id="VAR_026157"
FT VARIANT 348
FT /note="A -> T (in dbSNP:rs17856829)"
FT /evidence="ECO:0000269|PubMed:12623849,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:27227454"
FT /id="VAR_025860"
FT VARIANT 379
FT /note="F -> S"
FT /evidence="ECO:0000269|PubMed:11465086,
FT ECO:0000269|PubMed:14692971"
FT /id="VAR_026158"
FT VARIANT 431
FT /note="G -> R (in dbSNP:rs78718189)"
FT /evidence="ECO:0000269|PubMed:27227454"
FT /id="VAR_079756"
FT CONFLICT 89
FT /note="H -> Y (in Ref. 3; CAC83724)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="G -> V (in Ref. 3; CAC83724)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="I -> F (in Ref. 3; CAC83724)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..205
FT /note="NR -> DM (in Ref. 3; CAC83724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 46363 MW; 3D4716F221934910 CRC64;
MSAVLLLALL GFILPLPGVQ ALLCQFGTVQ HVWKVSDLPR QWTPKNTSCD SGLGCQDTLM
LIESGPQVSL VLSKGCTEAK DQEPRVTEHR MGPGLSLISY TFVCRQEDFC NNLVNSLPLW
APQPPADPGS LRCPVCLSME GCLEGTTEEI CPKGTTHCYD GLLRLRGGGI FSNLRVQGCM
PQPGCNLLNG TQEIGPVGMT ENCNRKDFLT CHRGTTIMTH GNLAQEPTDW TTSNTEMCEV
GQVCQETLLL LDVGLTSTLV GTKGCSTVGA QNSQKTTIHS APPGVLVASY THFCSSDLCN
SASSSSVLLN SLPPQAAPVP GDRQCPTCVQ PLGTCSSGSP RMTCPRGATH CYDGYIHLSG
GGLSTKMSIQ GCVAQPSSFL LNHTRQIGIF SAREKRDVQP PASQHEGGGA EGLESLTWGV
GLALAPALWW GVVCPSC
