SPB10_PAPAN
ID SPB10_PAPAN Reviewed; 397 AA.
AC A9RA96;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Serpin B10;
GN Name=SERPINB10;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protease inhibitor that may play a role in the regulation of
CC protease activities during hematopoiesis and apoptosis induced by TNF.
CC May regulate protease activities in the cytoplasm and in the nucleus
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; DP000514; ABX89278.1; -; Genomic_DNA.
DR RefSeq; NP_001162388.1; NM_001168917.1.
DR AlphaFoldDB; A9RA96; -.
DR SMR; A9RA96; -.
DR STRING; 9555.ENSPANP00000000198; -.
DR MEROPS; I04.015; -.
DR PRIDE; A9RA96; -.
DR Ensembl; ENSPANT00000007415; ENSPANP00000000198; ENSPANG00000009799.
DR GeneID; 100137382; -.
DR KEGG; panu:100137382; -.
DR CTD; 5273; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161205; -.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000028761; Chromosome 19.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..397
FT /note="Serpin B10"
FT /id="PRO_0000355548"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 74..77
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 362..363
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 45383 MW; 4DE80A27D4F553F0 CRC64;
MDTLATSINQ FALELSKKLA ESAQGKNIFF SSWSISTSLA MVYLGTKGTT AAQMGQVLQF
NRDQGVKSSP ESEKKRKMEF NSSNSEEIHS DFHTLISEIL KPNDDYLLKT ANAIYGEKTY
PFHNKYLEDM KTYFGAEPQS VNFVEASDQI RKEINSWVER QTEGKIQNLL PDDSVDSTTR
MILVNALYFK GIWEHQFLVQ NTTEKPFRIN ETTSKPVQMM FMKKKLQIFH IEKPQAVGLQ
LYYKSRDLSL LILLPEDING LVQLEKDITY EKLNEWTSAD MMELYEVQLH LPKFKLEDSY
DLKSTLSSMG MSDAFSQSKA DFSGMSSARN LFLSNVFHKA FVEINEQGTE AAAGTGSEIE
SRIRVPSIEF NANHPFLFFI RHNKTNSILF YGRLCSP