NGP_MOUSE
ID NGP_MOUSE Reviewed; 167 AA.
AC O08692; Q61903;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Neutrophilic granule protein {ECO:0000312|EMBL:AAI19404.1, ECO:0000312|MGI:MGI:105983};
DE Short=NGP {ECO:0000312|MGI:MGI:105983};
DE AltName: Full=Cystatin-like protein {ECO:0000303|PubMed:21518852};
DE AltName: Full=Myeloid bactenecin protein {ECO:0000303|PubMed:8839844, ECO:0000312|EMBL:AAB53634.1};
DE AltName: Full=Myeloid secondary granule protein {ECO:0000303|PubMed:8749713, ECO:0000312|EMBL:AAC42088.1};
DE Flags: Precursor;
GN Name=Ngp {ECO:0000312|EMBL:AAI19404.1,
GN ECO:0000312|Ensembl:ENSMUSP00000035061, ECO:0000312|MGI:MGI:105983};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=CBA/J {ECO:0000312|EMBL:AAC42088.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAC42088.1};
RX PubMed=8749713; DOI=10.1002/jcb.240590404;
RA Moscinski L.C., Hill B.;
RT "Molecular cloning of a novel myeloid granule protein.";
RL J. Cell. Biochem. 59:431-442(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MDF1 {ECO:0000312|EMBL:AAB53634.1};
RX PubMed=8839844;
RA Scott L.M., Mueller L., Collins S.J.;
RT "E3, a hematopoietic-specific transcript directly regulated by the retinoic
RT acid receptor alpha.";
RL Blood 88:2517-2530(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26414.1};
RC TISSUE=Tongue {ECO:0000312|EMBL:BAB26414.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mixed {ECO:0000312|EMBL:EDL09016.1};
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI19404.1};
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 34-42; 50-82; 86-96 AND 107-166, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, TISSUE SPECIFICITY, INDUCTION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=21518852; DOI=10.1096/fj.10-180604;
RA Boutte A.M., Friedman D.B., Bogyo M., Min Y., Yang L., Lin P.C.;
RT "Identification of a myeloid-derived suppressor cell cystatin-like protein
RT that inhibits metastasis.";
RL FASEB J. 25:2626-2637(2011).
RN [8]
RP INDUCTION.
RX PubMed=12515729; DOI=10.1182/blood-2002-04-1039;
RA Gombart A.F., Kwok S.H., Anderson K.L., Yamaguchi Y., Torbett B.E.,
RA Koeffler H.P.;
RT "Regulation of neutrophil and eosinophil secondary granule gene expression
RT by transcription factors C/EBP epsilon and PU.1.";
RL Blood 101:3265-3273(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a
CC role as a negative regulator of tumor vascular development, cell
CC invasion and metastasis. {ECO:0000269|PubMed:21518852}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked.
CC {ECO:0000269|PubMed:21518852}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}.
CC Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in
CC cytoplasmic granules of neutrophilic precursors (PubMed:8749713).
CC {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
CC -!- TISSUE SPECIFICITY: Expressed in myeloid bone marrow cells. Expressed
CC in neutrophilic precursors (at protein level) (PubMed:8749713).
CC Expressed in myeloid bone marrow cells (PubMed:21518852).
CC {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
CC -!- INDUCTION: Up-regulated by CCAAT/enhancer-binding proteins CEBPA and
CC CEBPE and transcription factor SPI1 (at protein level)
CC (PubMed:12515729). Down-regulated in malignant tumor conditioned medium
CC (PubMed:21518852). Up-regulated during early bone marrow
CC differentiation by the granulocyte-macrophage colony-stimulating factor
CC CSF2 and down-regulated during granulocytic maturation
CC (PubMed:8749713). {ECO:0000269|PubMed:12515729,
CC ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; L37297; AAC42088.1; -; mRNA.
DR EMBL; U95002; AAB53634.1; -; mRNA.
DR EMBL; AK009649; BAB26414.1; -; mRNA.
DR EMBL; AC160104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466621; EDL09016.1; -; Genomic_DNA.
DR EMBL; BC119403; AAI19404.1; -; mRNA.
DR EMBL; BC119405; AAI19406.1; -; mRNA.
DR CCDS; CCDS23566.1; -.
DR RefSeq; NP_032720.2; NM_008694.2.
DR AlphaFoldDB; O08692; -.
DR SMR; O08692; -.
DR STRING; 10090.ENSMUSP00000035061; -.
DR TCDB; 1.C.33.1.7; the cathelicidin (cathelicidin) family.
DR iPTMnet; O08692; -.
DR PhosphoSitePlus; O08692; -.
DR MaxQB; O08692; -.
DR PaxDb; O08692; -.
DR PeptideAtlas; O08692; -.
DR PRIDE; O08692; -.
DR ProteomicsDB; 287420; -.
DR DNASU; 18054; -.
DR Ensembl; ENSMUST00000035061; ENSMUSP00000035061; ENSMUSG00000032484.
DR GeneID; 18054; -.
DR KEGG; mmu:18054; -.
DR UCSC; uc009rtz.2; mouse.
DR CTD; 18054; -.
DR MGI; MGI:105983; Ngp.
DR VEuPathDB; HostDB:ENSMUSG00000032484; -.
DR eggNOG; ENOG502SU6N; Eukaryota.
DR GeneTree; ENSGT00730000111701; -.
DR HOGENOM; CLU_121724_1_0_1; -.
DR InParanoid; O08692; -.
DR OMA; CAFREDG; -.
DR OrthoDB; 1370632at2759; -.
DR PhylomeDB; O08692; -.
DR TreeFam; TF338457; -.
DR BioGRID-ORCS; 18054; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ngp; mouse.
DR PRO; PR:O08692; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O08692; protein.
DR Bgee; ENSMUSG00000032484; Expressed in granulocyte and 110 other tissues.
DR Genevisible; O08692; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:1901491; P:negative regulation of lymphangiogenesis; IDA:UniProtKB.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR001894; Cathelicidin-like.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR10206; PTHR10206; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Secreted; Signal; Thiol protease inhibitor;
KW Tumor suppressor.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..167
FT /note="Neutrophilic granule protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432423"
FT REGION 122..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 92
FT /note="D -> N (in Ref. 1; AAC42088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19332 MW; C742B385F095B6C1 CRC64;
MAGLWKTFVL VVALAVVSCE ALRQLRYEEI VDRAIEAYNQ GRQGRPLFRL LSATPPSSQN
PATNIPLQFR IKETECTSTQ ERQPKDCDFL EDGEERNCTG KFFRRRQSTS LTLTCDRDCS
REDTQETSFN DKQDVSEKEK FEDVPPHIRN IYEDAKYDII GNILKNF
