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Database: UniProt
Entry: A0A218UQ52_9PASE
LinkDB: A0A218UQ52_9PASE
Original site: A0A218UQ52_9PASE 
ID   A0A218UQ52_9PASE        Unreviewed;      1500 AA.
AC   A0A218UQ52;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Serpin B10 {ECO:0000256|ARBA:ARBA00041146};
GN   Name=SERPINB10 {ECO:0000313|EMBL:OWK55550.1};
GN   ORFNames=RLOC_00013761 {ECO:0000313|EMBL:OWK55550.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK55550.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK55550.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK55550.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000256|ARBA:ARBA00006426}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWK55550.1}.
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DR   EMBL; MUZQ01000197; OWK55550.1; -; Genomic_DNA.
DR   STRING; 299123.ENSLSDP00000018831; -.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd19956; serpinB; 2.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 3.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 4.
DR   Gene3D; 1.10.287.580; Helix hairpin bin; 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; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF175; SERPIN B10; 1.
DR   Pfam; PF00079; Serpin; 5.
DR   SMART; SM00093; SERPIN; 4.
DR   SUPFAM; SSF56574; Serpins; 4.
DR   PROSITE; PS00284; SERPIN; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619}.
FT   DOMAIN          13..398
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   DOMAIN          454..820
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   DOMAIN          830..1115
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   DOMAIN          1133..1500
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          868..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1500 AA;  170357 MW;  7E0E69F21E856A5E CRC64;
     MDTLNKANTS FALDFFKQQC QEDDRKNILF SPWSISSALA TVYLGAKGNT ADQMAQVLHF
     NKAEGAKNVT TTIRMHVYSR TEESLSNRRA CFQKTEIGKS DNIHTGFKAL SFEINQPTRN
     YLLKSVNQLY GEKSLPFSKE YLFLAKKYYS AEPQSVDFVG AADAIRRNIN SSVEQQTEGK
     IQNLLPPASV DSLTRLVLIN ALYFKGNWAT KFEAAATRQR PFRINMHTTK TVPMMYLRDK
     FNLNYIESVQ ADVLELPYVN NDLSMFILLP SDISGLQKLE RELTFENLST WTNPELMEKM
     NMEVYLPRFT LEEKYDLKST LSRMGIQDAF TEGQADFTAM SKTGDLFLSQ VFHKCYLEVN
     EEGTEAAAAS SATLASRSLE TRLRNSHDFN EISSTTQPAG CPSLTLLHIF ASVFLMIFSL
     KLDTQCPIQS LSLVFYAEVV KMEVVSTSIG NFTIDLFNKL NESNKGKNIF FSPWSISAAL
     ALTYLGAKGT TATEMAEDPE NKQAADIHSG FKKLLTAMNK PRSTYSLKGA NRIYVEKTFL
     LLPTYIQLSK NYYKAEPQKI NFKTAPEQSG KEINTWVEKQ TEGKIKNLLS PRDVTSSTKL
     ILINAIYFKA EWEVKFKAED TELQPFRLSK NKTKPVKMMY TRKTFPVLIM ATMNFKMIEL
     PYVKRELSMF ILLPDDIKDN STGLEQLERE LTYEKLSEWT DSKKMTETLV DLYLPKFKME
     ERYDISDTLI RMGMHSAFSS NADFSGMTEN AIAISKVLHK SFVAVDEKGT EAAAATAVIV
     EVTSMPVAHV LKFRVDHPFY FFIRHNKSKS ILFFGVPMES LSVSTNSFTL DLYKKLNETS
     KGQNIFFSPW SIATALAMVH LGAKGDTANQ MAETAREEGS SETRRPSPAR PKKRKTDPEH
     EGAENIHSGF KKLLCDINKR RSTYLLKSAN RLYEEKTYPL LPTKTTPVHM MFLKDKFFIL
     HETTMKFRII ELPYVENELS MFVLLPDDIS DNTTGLELVE RELTYEKLSE WTKSDNMMKA
     EVDLYLPKLK LEENYDLKSP LSSMGIQNAF DPGQADFTGM SAKKDLFISQ VIHKAFVEIN
     EEGTEAAAAT VKRNFFQEVL NKMLLCLITS KYVTLCRLGS MESLCAANSA FAVDLLRKLC
     EKKSGQNVFF SPFSISSALS MVLLGSRGST EAQISKVLSL NNAQDAHNGY QSLLSEINDP
     NTKYILRTAN RLYGEKTFEF LPSFIESSQK SYHAGLEQMD FLHAWEDSRK QINGWVEERT
     EGKIQNLLAE GILDSLTRLV LVNAIYFKGN WEEQFNKQRT TERPFQINKN ETRPVQMMFK
     EANFNMTYIG DFETKILELP YVGNELSMII LLPDAIQDGS TGLERLEREL TYEKLIDWIN
     PEMMDSTKVR VSLPRFKLEE DYDLKPILSS MGMTDAFELG KADFSGISPG DNQLVLSEVV
     HKSFVEVNEE GTEAAAATGA VMMMRCAMIV PEFIADHPFL FFIRHNKTSS ILFCGRFCCP
//
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