ID A0A3P8NA51_ASTCA Unreviewed; 405 AA.
AC A0A3P8NA51;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Serpin H1 {ECO:0000256|ARBA:ARBA00013551};
DE AltName: Full=Collagen-binding protein {ECO:0000256|ARBA:ARBA00030441};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000001645.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000001645.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000001645.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Binds specifically to collagen. Could be involved as a
CC chaperone in the biosynthetic pathway of collagen.
CC {ECO:0000256|ARBA:ARBA00025405}.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR AlphaFoldDB; A0A3P8NA51; -.
DR Ensembl; ENSACLT00000001681.1; ENSACLP00000001645.1; ENSACLG00000001116.1.
DR GeneTree; ENSGT00940000156163; -.
DR Proteomes; UP000265100; Chromosome 10.
DR Bgee; ENSACLG00000001116; Expressed in spleen and 5 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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:SF27; SERPIN H1; 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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..405
FT /note="Serpin H1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018054027"
FT DOMAIN 39..396
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 405 AA; 45442 MW; 0C5B1A0855C66C48 CRC64;
MYCLSSCLLL ASAATSTSKD KVLSNHATIL ADSTANLAFS VYQSMVKDKN VENIIISPVV
VASSLGLVAL GGKASTASQV KTILNVAKVK DEHLHPSLAE LLIELSDPKT RNITWKISNR
LYGPSSVTFV EDFVKSSKKH YNCEHSKINF RDKKNAVNSI NEWAAKSTDG KLPEVTKNVE
KTDGAMIISA MFFKCHWDEQ FHHKMVDNRG FMVSRSYTVS VQMMHRTGLF GFYDDKDNKL
SILSMPLSHK KSTVVFIMPY HVEPLDRLEK MLTKKQVDKW IGLLQETAIA VSLPKVSMEV
SHDLQKHLQE LGLTEAVDKS KADFSNISGK KDLYLSSVFH ASALEWDTDG NEIDTSIFGT
DKLKNPKLFY ADHPFIFLVK DQKTSSILFI GRMVRPKGEK MRDEL
//
