ID W5KG87_ASTMX Unreviewed; 401 AA.
AC W5KG87;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Serpin H1 {ECO:0000256|ARBA:ARBA00013551};
DE AltName: Full=Collagen-binding protein {ECO:0000256|ARBA:ARBA00030441};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000006599.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000006599.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; W5KG87; -.
DR MEROPS; I04.035; -.
DR Ensembl; ENSAMXT00000006599.2; ENSAMXP00000006599.2; ENSAMXG00000006432.2.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000156163; -.
DR HOGENOM; CLU_023330_2_0_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000006432; Expressed in embryo and 14 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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..401
FT /note="Serpin H1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017457996"
FT DOMAIN 35..392
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 401 AA; 45175 MW; FB0CD6A4F34A4100 CRC64;
VWILLALCLL ASVRADKALS SHATILVDSS TNLAFDLYHN MAKEKDMENI LISPVVVASS
LGVVALGGKS NTATQVKTVL SGNKVKDENL HSSLAEILTE VSNSTARNVT WKISNRLYGP
SSVNFVDDFL KNSKKHYKYE HSKINFRDKR SAVKAINEWG SKSTDGKLPE ITKDVEKTDG
AMIINAMFYK PHWDQQFHHK MVDNRGFLVH RSFTVSVPMM HRTGIYGFLE DTTNNLFVLE
MPLAHKMSSV VFIMTYHVEP LERVEKLLTR KQVETWLSKL EQKAVAVSLP KVSMEVSHNL
QKHLGELGLT EAVDKTKADL SNISGKKELY LSNVFHASAL EWDTEGNPPD TSVFGSDKLK
NPKLFYADHP FIFLVKDNKT KSILYIGRLV RPKGDKMRDE L
//
