ID A0A3L8SW39_CHLGU Unreviewed; 413 AA.
AC A0A3L8SW39;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
GN ORFNames=DV515_00002002 {ECO:0000313|EMBL:RLW10026.1};
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:RLW10026.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW10026.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW10026.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW10026.1};
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.
CC {ECO:0000256|RuleBase:RU000411}.
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:RLW10026.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QUSF01000004; RLW10026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SW39; -.
DR STRING; 44316.ENSEGOP00005000649; -.
DR Ensembl; ENSEGOT00005000740; ENSEGOP00005000649; ENSEGOG00005000552.
DR OMA; IHSNSYC; -.
DR Proteomes; UP000276834; 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; cd19957; serpinA; 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 Gene3D; 2.10.310.10; Serpins superfamily; 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:SF389; SERPIN DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..413
FT /note="Serpin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018059041"
FT DOMAIN 55..409
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 413 AA; 47463 MW; 0413A8430F39F099 CRC64;
MKMLLFLCLL LVGIHSNIYC YEPYQQGVRN QNQRAQENQN MPLQSVRNSV CRFACCFYKE
ISSRENNGNV FFSPLSISTA FAMLTLGARS DTLTQILRVL CFNPRQISEN DIHEGYHQLM
QMVNRRNGGL QLNMGNVLFV LDRLKPQDRF LNNLRNFYEG EAYPMNFKKA DQAQLKINEY
VARRTNGKIR DLVNNLDPLT EILLISYIYF NAEWEKPFDP KYTKMSKFFA DGNKVVEVPM
MFGMGLFKHG YDEQLSSTVV QMDYKGGASA FFILPDRGRM RKLEKRLSCE HLSRWSTLVT
KSSVNLYLPK FTLYGTYNLK DILYKMGIMD LFTDKADLSG ITGQPQHRIS QAIHKAVVKV
DETGTEAAAA TGMEIVPMSV PVTVRFNRPF LMVIIMDNTI LFMGKIVNPL KKN
//
