ID   NEUS_RAT                Reviewed;         410 AA.
AC   Q9JLD2; Q9JLD1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 141.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RC   TISSUE=Pituitary;
RX   PubMed=10642518; DOI=10.1042/bj3450595;
RA   Hill R.M., Parmar P.K., Coates L.C., Mezey E., Pearson J.F., Birch N.P.;
RT   "Neuroserpin is expressed in the pituitary and adrenal glands and induces
RT   the extension of neurite-like processes in AtT-20 cells.";
RL   Biochem. J. 345:595-601(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits plasminogen
CC       activators and plasmin but not thrombin. May be involved in the
CC       formation or reorganization of synaptic connections as well as for
CC       synaptic plasticity in the adult nervous system. May protect neurons
CC       from cell damage by tissue-type plasminogen activator.
CC       {ECO:0000305|PubMed:10642518}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10642518}.
CC       Cytoplasmic vesicle, secretory vesicle lumen
CC       {ECO:0000250|UniProtKB:Q99574}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q99574}.
CC   -!- TISSUE SPECIFICITY: Detected in adult pituitary and adrenal gland.
CC       {ECO:0000269|PubMed:10642518}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; AF193014; AAF70386.1; -; mRNA.
DR   EMBL; AF193015; AAF70387.1; -; mRNA.
DR   EMBL; BC061536; AAH61536.1; -; mRNA.
DR   RefSeq; NP_446231.1; NM_053779.1.
DR   RefSeq; XP_008759298.1; XM_008761076.2.
DR   AlphaFoldDB; Q9JLD2; -.
DR   SMR; Q9JLD2; -.
DR   STRING; 10116.ENSRNOP00000013905; -.
DR   MEROPS; I04.025; -.
DR   GlyCosmos; Q9JLD2; 3 sites, No reported glycans.
DR   GlyGen; Q9JLD2; 4 sites.
DR   iPTMnet; Q9JLD2; -.
DR   PhosphoSitePlus; Q9JLD2; -.
DR   PaxDb; 10116-ENSRNOP00000013905; -.
DR   Ensembl; ENSRNOT00000013904.7; ENSRNOP00000013905.4; ENSRNOG00000010248.7.
DR   Ensembl; ENSRNOT00055002446; ENSRNOP00055001854; ENSRNOG00055001513.
DR   Ensembl; ENSRNOT00060011722; ENSRNOP00060008825; ENSRNOG00060007133.
DR   Ensembl; ENSRNOT00065022448; ENSRNOP00065017405; ENSRNOG00065013647.
DR   GeneID; 116459; -.
DR   KEGG; rno:116459; -.
DR   UCSC; RGD:619896; rat.
DR   AGR; RGD:619896; -.
DR   CTD; 5274; -.
DR   RGD; 619896; Serpini1.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000158168; -.
DR   HOGENOM; CLU_023330_0_4_1; -.
DR   InParanoid; Q9JLD2; -.
DR   OMA; IQNGFHV; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q9JLD2; -.
DR   TreeFam; TF352620; -.
DR   PRO; PR:Q9JLD2; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000010248; Expressed in Ammon's horn and 15 other cell types or tissues.
DR   GO; GO:0060205; C:cytoplasmic vesicle lumen; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0034774; C:secretory granule lumen; ISO:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
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; Q9JLD2; RN.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Glycoprotein; Phosphoprotein; 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_0000032523"
FT   SITE            362..363
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:Q99574"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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        12
FT                   /note="L -> M (in Ref. 1; AAF70387)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="H -> Q (in Ref. 1; AAF70387)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  46278 MW;  99008624B3A366D8 CRC64;
     MAYLGLLSLV ALQSLVTGAA FPDETIAEWS VNVYNHLRAT GEDENILFSP LSIALAMGVM
     ELGAQGSTLK EIRHSMGYES LKSGEEFSFL RDFSSMVSAE EGQYVMKIAN SLFVQNGFHI
     NEEFLQMMKM YFNAEVNHVD FSENVAVANY INKWVENYTN SLLKDLVSPG DFDAVTHLAL
     INAVYFKGNW KSQFRPENTR TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ
     VLEIPYEGDE ISMMLVLSRQ EVPLATLEPL LKPQLIEEWA NSVKKQKVEV YLPRFTVEQE
     IDLKDILKAL GVTEIFIKDA NLTAMSDKKE LFLSKAVHKS FIEVNEEGSE AAVASGMIAI
     SRMAVLFPQV IVDHPFLFLI KNRKTGTILF MGRVMHPETM NTSGHDFEEL
//