NEUS_RAT
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 03-AUG-2022, entry version 133.
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 GlyGen; Q9JLD2; 3 sites.
DR iPTMnet; Q9JLD2; -.
DR PhosphoSitePlus; Q9JLD2; -.
DR PaxDb; Q9JLD2; -.
DR Ensembl; ENSRNOT00000013904; ENSRNOP00000013905; ENSRNOG00000010248.
DR GeneID; 116459; -.
DR KEGG; rno:116459; -.
DR UCSC; RGD:619896; rat.
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; KDVWRGL; -.
DR OrthoDB; 1124079at2759; -.
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 tissues.
DR Genevisible; Q9JLD2; RN.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:RGD.
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 Cytoplasmic vesicle; Glycoprotein; Phosphoprotein; 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_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 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
