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   27-MAR-2024, entry version 180.
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   GlyCosmos; O35684; 3 sites, 3 glycans.
DR   GlyGen; O35684; 4 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; O35684; -.
DR   PhosphoSitePlus; O35684; -.
DR   EPD; O35684; -.
DR   MaxQB; O35684; -.
DR   PaxDb; 10090-ENSMUSP00000029423; -.
DR   PeptideAtlas; O35684; -.
DR   ProteomicsDB; 252954; -.
DR   Antibodypedia; 987; 522 antibodies from 39 providers.
DR   DNASU; 20713; -.
DR   Ensembl; ENSMUST00000029423.9; ENSMUSP00000029423.9; ENSMUSG00000027834.16.
DR   GeneID; 20713; -.
DR   KEGG; mmu:20713; -.
DR   UCSC; uc008pne.2; mouse.
DR   AGR; MGI:1194506; -.
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; IQNGFHV; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; O35684; -.
DR   TreeFam; TF352620; -.
DR   BioGRID-ORCS; 20713; 1 hit in 77 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 211 other cell types or tissues.
DR   ExpressionAtlas; O35684; baseline and differential.
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:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   CDD; cd02048; serpinI1_NSP; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF50; NEUROSERPIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; O35684; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Glycoprotein; Protease inhibitor;
KW   Proteoglycan; Reference proteome; Secreted; Serine protease inhibitor;
KW   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   CARBOHYD        403
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99574"
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
//