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Database: UniProt
Entry: A0A3B3SVN6_9TELE
LinkDB: A0A3B3SVN6_9TELE
Original site: A0A3B3SVN6_9TELE 
ID   A0A3B3SVN6_9TELE        Unreviewed;       372 AA.
AC   A0A3B3SVN6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Serpin H1 {ECO:0000256|ARBA:ARBA00013551};
DE   AltName: Full=Collagen-binding protein {ECO:0000256|ARBA:ARBA00030441};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000034822.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000034822.1}
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; A0A3B3SVN6; -.
DR   Ensembl; ENSPKIT00000015745.1; ENSPKIP00000034822.1; ENSPKIG00000013898.1.
DR   GeneTree; ENSGT00940000156163; -.
DR   Proteomes; UP000261540; Unplaced.
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; 2.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 2.
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; 2.
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}.
FT   DOMAIN          31..363
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   372 AA;  42216 MW;  B586BF7537DE478E CRC64;
     MFCKRVIVCN TVVASPNKII EDNYKTKKYN LKLYHNMEND ASLKSENIFI SPVVLTSSLG
     VITLGARQNT ANQVKSLLNV PLVEDSIHIL LSKLLTDASD EAISDIDWKV SSRSYGPAWI
     NLSPDFVEKS EVHYRHNSSK VNFRDKWHHE NQQMDLPVID GALFINAMLL KPHWAEAFSH
     KMVDKRGFMI SGTRTVSVQM MHRTDEPNQL QFLEIPLGKM QSSLLILMPF HMEPLEKVLT
     KENIYRWSDQ LKEQAVAVSL PEADVGSIHE LQKYLKQLGL VEAVDKSKAD FSGITGKPDL
     PLSHFLHAAG CEIQTGGNEF DENIFGREEL KTPKLFYADH PFIFFVQDTK TNSILFLGRL
     LNPRNGGNHD EL
//
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