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Database: UniProt
Entry: H2ZYY1_LATCH
LinkDB: H2ZYY1_LATCH
Original site: H2ZYY1_LATCH 
ID   H2ZYY1_LATCH            Unreviewed;       430 AA.
AC   H2ZYY1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002602.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000002602.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; AFYH01145463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01145464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01145465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2ZYY1; -.
DR   STRING; 7897.ENSLACP00000002602; -.
DR   Ensembl; ENSLACT00000002623.1; ENSLACP00000002602.1; ENSLACG00000002328.1.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000160877; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; H2ZYY1; -.
DR   OMA; MVLINHI; -.
DR   TreeFam; TF343201; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000002328; Expressed in pharyngeal gill and 2 other cell types or tissues.
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:SF165; ALPHA-1-ANTITRYPSIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          70..428
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..45
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  49105 MW;  64868209EED1568C CRC64;
     GPHHGHHHSP HHGHHHSPHH GHRHGPHHGH HHSPHHGHHH DHHRHHHDLY NEDEDMLCHK
     LTPANSDFAI RFYNKVLSCP TRATKNIFFS PISISTALSM LSLGAKSSTL HQLHEGLGFN
     TTELSEDEIH KAFEHLILML NKDHNELQIN TGNVIYLNEG FEPIQKFIDD AKLYYDAEVS
     NVDFQKSEET MQKINAHVKN QTHGKIEDLI KDLDNDTIML LLNYIFFRGE WEKPFSPNAT
     EEGDFFVNND ITVKVPMMTR TSFFEAQYEK NISATILKLP YKGNATMMLI LPDEGKMEKV
     EKTLSHKVLM KWVFNKEHNF ITLNLPKFSI SASHELKEIL MEMGITDVFG DNSDPSGITE
     SPNLKVSKAV HKAILEVGEK GTEAGGTTHV GIIPLSLPGE VHFNRPFLMF IWHRLTRSIL
     FMGKIVNPTE
//
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