SPB10_CALJA
ID SPB10_CALJA Reviewed; 397 AA.
AC B0CMB0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Serpin B10;
GN Name=SERPINB10;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
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 (JAN-2008) 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; DP000562; ABY74571.1; -; Genomic_DNA.
DR RefSeq; XP_008978187.1; XM_008979939.2.
DR AlphaFoldDB; B0CMB0; -.
DR SMR; B0CMB0; -.
DR STRING; 9483.ENSCJAP00000012445; -.
DR MEROPS; I04.015; -.
DR PRIDE; B0CMB0; -.
DR GeneID; 100407965; -.
DR KEGG; cjc:100407965; -.
DR CTD; 5273; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; B0CMB0; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF352619; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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_0000355545"
FT MOTIF 74..77
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT SITE 362..363
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 45433 MW; F3DB5E81CDBB68E5 CRC64;
MDALATSINQ FALELSQKLA ESAQGKNIFF SAWSISASLA MVHLGAKGNT AAQMAQVLQF
KRDQGVKSDP ESEKKRKMEF NLSNSGEIHC NFQTLISEIL KPNNDYILKT ANATYSEKTY
PFHNKYLEDV KTYFGAEPQS VNFVEASDQI RKEINSWVER QTEGKIQNLL SDDSVDSTTR
MVLVNALYFK GIWEHQFLVQ HTTEKPFRIN ETTSKPVQMM FMKEKLQIFH IEKPQALGLQ
LYYKSRDLSL FILLPEDING LEQLEKAITY EKLNEWTSAD MMEVYHVQLH LPKFKLEESY
DLKSTLSSMG MRDAFSESKA DFSGMSSARN LFLSNVFHKA FVEIDEQGTE AAAGSGSEIS
FRMKVPSIEF NANHPFLFFI RHNKTNNILF YGRFCSP