NEUS_CHICK
ID NEUS_CHICK Reviewed; 410 AA.
AC Q90935; A0A1I7Q408;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neuroserpin;
DE AltName: Full=Axonin-2;
DE AltName: Full=Peptidase inhibitor 12;
DE Short=PI-12;
DE AltName: Full=Serpin I1;
DE Flags: Precursor;
GN Name=SERPINI1; Synonyms=PI12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=8670795; DOI=10.1002/j.1460-2075.1996.tb00657.x;
RA Osterwalder T., Contartese J., Stoeckli E.T., Kuhn T.B., Sonderegger P.;
RT "Neuroserpin, an axonally secreted serine protease inhibitor.";
RL EMBO J. 15:2944-2953(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP 362-ARG-MET-363, AND REACTIVE BOND.
RX PubMed=9442076; DOI=10.1074/jbc.273.4.2312;
RA Osterwalder T., Cinelli P., Baici A., Pennella A., Krueger S.R.,
RA Schrimpf S.P., Meins M., Sonderegger P.;
RT "The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits
RT plasminogen activators and plasmin but not thrombin.";
RL J. Biol. Chem. 273:2312-2321(1998).
CC -!- FUNCTION: Serine protease inhibitor that inhibits plasminogen
CC activators and plasmin but not thrombin (PubMed:9442076). May be
CC involved in the formation or reorganization of synaptic connections as
CC well as for synaptic plasticity in the adult nervous system. May
CC protect neurons from cell damage by tissue-type plasminogen activator
CC (Probable). {ECO:0000269|PubMed:9442076, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670795,
CC ECO:0000269|PubMed:9442076}. Cytoplasmic vesicle, secretory vesicle
CC lumen {ECO:0000250|UniProtKB:Q99574}. Perikaryon
CC {ECO:0000250|UniProtKB:Q99574}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic ocular vitreous fluid (at
CC protein level) (PubMed:9442076). In the embryo present in retina,
CC brain, cerebellum and spinal cord (PubMed:8670795). In adult,
CC predominantly expressed in the brain (PubMed:8670795).
CC {ECO:0000269|PubMed:8670795, ECO:0000269|PubMed:9442076}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; Z71930; CAA96493.1; -; mRNA.
DR EMBL; AADN04000312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S70647; S70647.
DR RefSeq; NP_001004411.1; NM_001004411.1.
DR RefSeq; XP_015147152.1; XM_015291666.1.
DR RefSeq; XP_015147153.1; XM_015291667.1.
DR AlphaFoldDB; Q90935; -.
DR SMR; Q90935; -.
DR STRING; 9031.ENSGALP00000015400; -.
DR MEROPS; I04.025; -.
DR PaxDb; Q90935; -.
DR PRIDE; Q90935; -.
DR GeneID; 425002; -.
DR KEGG; gga:425002; -.
DR CTD; 5274; -.
DR VEuPathDB; HostDB:geneid_425002; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; Q90935; -.
DR PhylomeDB; Q90935; -.
DR TreeFam; TF352620; -.
DR PRO; PR:Q90935; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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; Direct protein sequencing; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8670795"
FT CHAIN 17..410
FT /note="Neuroserpin"
FT /id="PRO_0000032524"
FT SITE 362..363
FT /note="Reactive bond"
FT /evidence="ECO:0000269|PubMed:9442076"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 362..363
FT /note="RM->EP: Loss of protease inhibitor activity."
FT /evidence="ECO:0000269|PubMed:9442076"
SQ SEQUENCE 410 AA; 46529 MW; D5B3B03E77F5FCE6 CRC64;
MYFLGLLSLL VLPSKAFKTN FPDETIAELS VNVYNQLRAA REDENILFCP LSIAIAMGMI
ELGAHGTTLK EIRHSLGFDS LKNGEEFTFL KDLSDMATTE ESHYVLNMAN SLYVQNGFHV
SEKFLQLVKK YFKAEVENID FSQSAAVATH INKWVENHTN NMIKDFVSSR DFSALTHLVL
INAIYFKGNW KSQFRPENTR TFSFTKDDET EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ
VLEIPYEGDE ISMMIVLSRQ EVPLVTLEPL VKASLINEWA NSVKKQKVEV YLPRFTVEQE
IDLKDVLKGL GITEVFSRSA DLTAMSDNKE LYLAKAFHKA FLEVNEEGSE AAAASGMIAI
SRMAVLYPQV IVDHPFFFLV RNRRTGTVLF MGRVMHPEAM NTSGHDFEEL
