ID   SERPH_CHICK             Reviewed;         405 AA.
AC   P13731; P29042;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Serpin H1;
DE   AltName: Full=47 kDa heat shock protein;
DE   AltName: Full=Collagen-binding protein;
DE            Short=Colligin;
DE   Flags: Precursor;
GN   Name=SERPINH1; Synonyms=HSP47;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 16-51; 117-134 AND
RP   159-177.
RC   TISSUE=Fibroblast;
RX   PubMed=2072906; DOI=10.1128/mcb.11.8.4036-4044.1991;
RA   Hirayoshi K., Kudo H., Takeuchi H., Nakai A., Iwamatsu A., Yamada K.M.,
RA   Nagata K.;
RT   "HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat
RT   shock protein of chicken embryo fibroblasts.";
RL   Mol. Cell. Biol. 11:4036-4044(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-51.
RX   PubMed=3377793; DOI=10.1016/s0006-291x(88)81242-7;
RA   Nagata K., Saga S., Yamada K.M.;
RT   "Characterization of a novel transformation-sensitive heat-shock protein
RT   (HSP47) that binds to collagen.";
RL   Biochem. Biophys. Res. Commun. 153:428-434(1988).
CC   -!- FUNCTION: Binds specifically to collagen. Could be involved as a
CC       chaperone in the biosynthetic pathway of collagen.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; X57157; CAA40444.1; -; mRNA.
DR   PIR; A41252; A41252.
DR   RefSeq; NP_990622.1; NM_205291.1.
DR   RefSeq; XP_015136452.1; XM_015280966.1.
DR   RefSeq; XP_015136453.1; XM_015280967.1.
DR   AlphaFoldDB; P13731; -.
DR   SMR; P13731; -.
DR   BioGRID; 676488; 1.
DR   IntAct; P13731; 1.
DR   STRING; 9031.ENSGALP00000018265; -.
DR   MEROPS; I04.035; -.
DR   PaxDb; P13731; -.
DR   PRIDE; P13731; -.
DR   Ensembl; ENSGALT00000018287; ENSGALP00000018265; ENSGALG00000011214.
DR   GeneID; 396228; -.
DR   KEGG; gga:396228; -.
DR   CTD; 871; -.
DR   VEuPathDB; HostDB:geneid_396228; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000156163; -.
DR   HOGENOM; CLU_023330_2_0_1; -.
DR   InParanoid; P13731; -.
DR   OMA; WDEKFHE; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; P13731; -.
DR   TreeFam; TF343094; -.
DR   Reactome; R-GGA-1650814; Collagen biosynthesis and modifying enzymes.
DR   PRO; PR:P13731; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000011214; Expressed in lung and 11 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   CDD; cd02046; serpinH1_CBP1; 1.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR033830; Serpin_H1_serpin_dom.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   InterPro; IPR033547; SERPINH1.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   PANTHER; PTHR11461:SF27; PTHR11461:SF27; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW   Reference proteome; Signal; Stress response.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:2072906,
FT                   ECO:0000269|PubMed:3377793"
FT   CHAIN           16..405
FT                   /note="Serpin H1"
FT                   /id="PRO_0000032519"
FT   MOTIF           402..405
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000305"
FT   SITE            364..365
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  45682 MW;  768318F3E9B59EFA CRC64;
     MQIFLVLALC GLAAAVPSED RKLSDKATTL ADRSTTLAFN LYHAMAKDKN MENILLSPVV
     VASSLGLVSL GGKATTASQA KAVLSADKLN DDYVHSGLSE LLNEVSNSTA RNVTWKIGNR
     LYGPASINFA DDFVKNSKKH YNYEHSKINF RDKRSALKSI NEWAAQTTDG KLPEVTKDVE
     KTDGALIVNA MFFKPHWDEK FHHKMVDNRG FMVTRSYTVG VPMMHRTGLY NYYDDEAEKL
     QVVEMPLAHK LSSMIFIMPN HVEPLERVEK LLNREQLKTW ASKMKKRSVA ISLPKVVLEV
     SHDLQKHLAD LGLTEAIDKT KADLSKISGK KDLYLSNVFH AAALEWDTDG NPYDADIYGR
     EEMRNPKLFY ADHPFIFMIK DSKTNSILFI GRLVRPKGDK MRDEL