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SERA_MANSE
ID   SERA_MANSE              Reviewed;         392 AA.
AC   P14754;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Alaserpin;
DE   AltName: Full=Serpin-1;
DE   Flags: Precursor;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hemolymph;
RX   PubMed=2463253; DOI=10.1016/s0021-9258(19)85038-x;
RA   Kanost M.R., Prasad S.V., Wells M.A.;
RT   "Primary structure of a member of the serpin superfamily of proteinase
RT   inhibitors from an insect, Manduca sexta.";
RL   J. Biol. Chem. 264:965-972(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hemocyte;
RX   PubMed=8276850; DOI=10.1016/s0021-9258(17)42311-8;
RA   Jiang H., Kanost M.R.;
RT   "Mutually exclusive exon use and reactive center diversity in insect
RT   serpins.";
RL   J. Biol. Chem. 269:55-58(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8910411; DOI=10.1074/jbc.271.45.28017;
RA   Jiang H., Wang Y., Huang Y., Mulnix A.B., Kadel J., Cole K., Kanost M.R.;
RT   "Organization of serpin gene-1 from Manduca sexta. Evolution of a family of
RT   alternate exons encoding the reactive site loop.";
RL   J. Biol. Chem. 271:28017-28023(1996).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=14728663; DOI=10.1111/j.1365-2583.2004.00454.x;
RA   Gorman M.J., Kankanala P., Kanost M.R.;
RT   "Bacterial challenge stimulates innate immune responses in extra-embryonic
RT   tissues of tobacco hornworm eggs.";
RL   Insect Mol. Biol. 13:19-24(2004).
CC   -!- FUNCTION: Inhibits elastase.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=P14754-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- DEVELOPMENTAL STAGE: Expressed in naive 2 h (precellular blastoderm
CC       stage) and 24 h (predorsal closure stage) eggs.
CC       {ECO:0000269|PubMed:14728663}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:14728663}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; M23438; AAA29327.1; -; mRNA.
DR   EMBL; L20792; AAA29329.1; -; mRNA.
DR   EMBL; U58361; AAC47343.1; -; Genomic_DNA.
DR   PIR; A38829; A38829.
DR   PDB; 1K9O; X-ray; 2.30 A; I=15-392.
DR   PDB; 1SEK; X-ray; 2.10 A; A=15-354.
DR   PDBsum; 1K9O; -.
DR   PDBsum; 1SEK; -.
DR   AlphaFoldDB; P14754; -.
DR   SMR; P14754; -.
DR   IntAct; P14754; 1.
DR   MINT; P14754; -.
DR   MEROPS; I04.031; -.
DR   EvolutionaryTrace; P14754; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR015557; Serpin_B1.
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   PANTHER; PTHR11461:SF180; PTHR11461:SF180; 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; Alternative splicing; Glycoprotein; Protease inhibitor;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..392
FT                   /note="Alaserpin"
FT                   /id="PRO_0000032527"
FT   SITE            359..360
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           25..41
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          107..117
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           144..158
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          178..188
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          212..228
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            229..232
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          233..240
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          244..254
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           258..264
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            268..276
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          279..288
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          290..297
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   HELIX           298..303
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   TURN            319..321
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          331..341
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          349..351
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          354..359
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:1K9O"
FT   STRAND          373..390
FT                   /evidence="ECO:0007829|PDB:1K9O"
SQ   SEQUENCE   392 AA;  43510 MW;  5138617BDE7EDA7A CRC64;
     MKIIMCIFGL AALAMAGETD LQKILRESND QFTAQMFSEV VKANPGQNVV LSAFSVLPPL
     GQLALASVGE SHDELLRALA LPNDNVTKDV FADLNRGVRA VKGVDLKMAS KIYVAKGLEL
     NDDFAAVSRD VFGSEVQNVD FVKSVEAAGA INKWVEDQTN NRIKNLVDPD ALDETTRSVL
     VNAIYFKGSW KDKFVKERTM DRDFHVSKDK TIKVPTMIGK KDVRYADVPE LDAKMIEMSY
     EGDQASMIII LPNQVDGITA LEQKLKDPKA LSRAEERLYN TEVEIYLPKF KIETTTDLKE
     VLSNMNIKKL FTPGAARLEN LLKTKESLYV DAAIQKAFIE VNEEGAEAAA ANAFGIVPAS
     LILYPEVHID RPFYFELKID GIPMFNGKVI EP
 
 
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