NEUS_MOUSE
ID NEUS_MOUSE Reviewed; 410 AA.
AC O35684; Q543F7; Q922U6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Neuroserpin;
DE AltName: Full=Peptidase inhibitor 12;
DE Short=PI-12;
DE AltName: Full=Serine protease inhibitor 17;
DE AltName: Full=Serpin I1;
DE Flags: Precursor;
GN Name=Serpini1; Synonyms=Pi12, Spi17;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9364046; DOI=10.1523/jneurosci.17-23-08984.1997;
RA Krueger S.R., Ghisu G.-P., Cinelli P., Gschwend T.P., Osterwalder T.,
RA Wolfer D.P., Sonderegger P.;
RT "Expression of neuroserpin, an inhibitor of tissue plasminogen activator,
RT in the developing and adult nervous system of the mouse.";
RL J. Neurosci. 17:8984-8996(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP GENE STRUCTURE.
RX PubMed=9729122; DOI=10.1016/s0378-1119(98)00255-8;
RA Berger P., Kozlov S.V., Krueger S.R., Sonderegger P.;
RT "Structure of the mouse gene for the serine protease inhibitor neuroserpin
RT (PI12).";
RL Gene 214:25-33(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17040209; DOI=10.1042/bj20061170;
RA Ishigami S., Sandkvist M., Tsui F., Moore E., Coleman T.A., Lawrence D.A.;
RT "Identification of a novel targeting sequence for regulated secretion in
RT the serine protease inhibitor neuroserpin.";
RL Biochem. J. 402:25-34(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS), FUNCTION, AND REACTIVE BOND.
RX PubMed=11557034; DOI=10.1016/s0014-5793(01)02764-8;
RA Briand C., Kozlov S.V., Sonderegger P., Gruetter M.G.;
RT "Crystal structure of neuroserpin: a neuronal serpin involved in a
RT conformational disease.";
RL FEBS Lett. 505:18-22(2001).
CC -!- FUNCTION: Serine protease inhibitor that inhibits plasminogen
CC activators and plasmin but not thrombin (PubMed:9364046,
CC PubMed:11557034). May be involved in the formation or reorganization of
CC synaptic connections as well as for synaptic plasticity in the adult
CC nervous system. May protect neurons from cell damage by tissue-type
CC plasminogen activator (Probable). {ECO:0000269|PubMed:11557034,
CC ECO:0000269|PubMed:9364046, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q90935}.
CC Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000269|PubMed:17040209}. Perikaryon
CC {ECO:0000269|PubMed:17040209}.
CC -!- TISSUE SPECIFICITY: Detected in neurons in embryonic brain cortex (at
CC protein level) (PubMed:17040209). During embryonic development mostly
CC expressed in CNS (PubMed:9364046). In adult expressed in brain and much
CC less in spinal cord, heart, kidney and testis (PubMed:9364046).
CC {ECO:0000269|PubMed:17040209, ECO:0000269|PubMed:9364046}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AJ001700; CAA04939.1; -; mRNA.
DR EMBL; AK032152; BAC27727.1; -; mRNA.
DR EMBL; AK051756; BAC34756.1; -; mRNA.
DR EMBL; BC006776; AAH06776.1; -; mRNA.
DR CCDS; CCDS17415.1; -.
DR RefSeq; NP_033276.1; NM_009250.2.
DR PDB; 1JJO; X-ray; 3.06 A; A/B=25-64, C/D=101-361, E/F=367-397.
DR PDBsum; 1JJO; -.
DR AlphaFoldDB; O35684; -.
DR SMR; O35684; -.
DR STRING; 10090.ENSMUSP00000029423; -.
DR MEROPS; I04.025; -.
DR GlyConnect; 2558; 3 N-Linked glycans (1 site).
DR GlyGen; O35684; 3 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; O35684; -.
DR EPD; O35684; -.
DR MaxQB; O35684; -.
DR PaxDb; O35684; -.
DR PeptideAtlas; O35684; -.
DR PRIDE; O35684; -.
DR ProteomicsDB; 252954; -.
DR Antibodypedia; 987; 478 antibodies from 39 providers.
DR DNASU; 20713; -.
DR Ensembl; ENSMUST00000029423; ENSMUSP00000029423; ENSMUSG00000027834.
DR GeneID; 20713; -.
DR KEGG; mmu:20713; -.
DR UCSC; uc008pne.2; mouse.
DR CTD; 5274; -.
DR MGI; MGI:1194506; Serpini1.
DR VEuPathDB; HostDB:ENSMUSG00000027834; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158168; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; O35684; -.
DR OMA; KDVWRGL; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; O35684; -.
DR TreeFam; TF352620; -.
DR BioGRID-ORCS; 20713; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Serpini1; mouse.
DR EvolutionaryTrace; O35684; -.
DR PRO; PR:O35684; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35684; protein.
DR Bgee; ENSMUSG00000027834; Expressed in retrosplenial region and 208 other tissues.
DR ExpressionAtlas; O35684; baseline and differential.
DR Genevisible; O35684; MM.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0034774; C:secretory granule lumen; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..410
FT /note="Neuroserpin"
FT /id="PRO_0000032522"
FT SITE 362..363
FT /note="Reactive bond"
FT /evidence="ECO:0000305|PubMed:11557034"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="E -> G (in Ref. 3; AAH06776)"
FT /evidence="ECO:0000305"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1JJO"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:1JJO"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 178..190
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1JJO"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1JJO"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 346..358
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:1JJO"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:1JJO"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:1JJO"
SQ SEQUENCE 410 AA; 46348 MW; DA3AF6F5195EBB7C CRC64;
MTYLELLALL ALQSVVTGAT FPDETITEWS VNMYNHLRGT GEDENILFSP LSIALAMGMM
ELGAQGSTRK EIRHSMGYEG LKGGEEFSFL RDFSNMASAE ENQYVMKLAN SLFVQNGFHV
NEEFLQMLKM YFNAEVNHVD FSQNVAVANS INKWVENYTN SLLKDLVSPE DFDGVTNLAL
INAVYFKGNW KSQFRPENTR TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ
VLEIPYEGDE ISMMLALSRQ EVPLATLEPL LKAQLIEEWA NSVKKQKVEV YLPRFTVEQE
IDLKDILKAL GVTEIFIKDA NLTAMSDKKE LFLSKAVHKS CIEVNEEGSE AAAASGMIAI
SRMAVLYPQV IVDHPFLYLI RNRKSGIILF MGRVMNPETM NTSGHDFEEL
