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Database: UniProt
Entry: A0A3L8SNW0_CHLGU
LinkDB: A0A3L8SNW0_CHLGU
Original site: A0A3L8SNW0_CHLGU 
ID   A0A3L8SNW0_CHLGU        Unreviewed;       376 AA.
AC   A0A3L8SNW0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
GN   ORFNames=DV515_00005754 {ECO:0000313|EMBL:RLW04464.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW04464.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW04464.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW04464.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW04464.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
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:RLW04464.1}.
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DR   EMBL; QUSF01000013; RLW04464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SNW0; -.
DR   STRING; 44316.ENSEGOP00005008533; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd19956; serpinB; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF186; SERPIN B4; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..376
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   376 AA;  43250 MW;  924DC89419C6CBD0 CRC64;
     MCSLSAANAK FCLDFFRELN KRKRNENIFF SPLSLSAAFG MVVLGARGST LEQIEKCEED
     EGVHSQFQAL LAEVSEPGPG CCLTIANRLF GEMTYPFFQK YLDSTKKFYR AELEPVNFKY
     TEEEVRDKIN FWVENETKGK IKDLFAAGFI DPSTVLVLVN AIYFKGKWAV EFKKEDTKEA
     YFHLNKNERR KVQMMFQEGY FNMAIIEELK TKVIELQYFN NELSMFILLP EDDCEDFTGL
     EQLECALTYE KLAEWTSLAT MQPLRVKVFL PQFKMEESYV LNNTLQEMGV MNVFDWGKAD
     LSGISMKDGL AVSKAIQKTI VEVNEEGTEA GCSMELLAMP LCCPVTCEFR ADHPFLFFIR
     HNQTNTILFF GRYSSP
//
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