ID   SERPH_RAT               Reviewed;         417 AA.
AC   P29457;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   04-NOV-2026, entry version 152.
DE   RecName: Full=Serpin H1;
DE   AltName: Full=47 kDa heat shock protein;
DE   AltName: Full=Collagen-binding protein;
DE            Short=Colligin;
DE   AltName: Full=GP46;
DE   Flags: Precursor;
GN   Name=Serpinh1; Synonyms=Cbp1, Hsp47;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-41; 167-192 AND
RP   339-352.
RX   PubMed=1654327; DOI=10.1016/s0021-9258(19)47363-8;
RA   Clarke E.P., Cates G.A., Ball E.H., Sanwal B.D.;
RT   "A collagen-binding protein in the endoplasmic reticulum of myoblasts
RT   exhibits relationship with serine protease inhibitors.";
RL   J. Biol. Chem. 266:17230-17235(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 18-33.
RX   PubMed=2158279; DOI=10.1016/0003-9861(90)90263-x;
RA   Nanden D., Cates G.A., Ball E.H., Sanwal B.D.;
RT   "Partial characterization of a collagen-binding, differentiation-related
RT   glycoprotein from skeletal myoblasts.";
RL   Arch. Biochem. Biophys. 278:291-296(1990).
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 and retinoic acid.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; M69246; AAA41270.1; -; mRNA.
DR   PIR; A40968; A40968.
DR   RefSeq; NP_058869.2; NM_017173.2.
DR   AlphaFoldDB; P29457; -.
DR   SMR; P29457; -.
DR   BioGRID; 248001; 4.
DR   ELM; P29457; -.
DR   FunCoup; P29457; 916.
DR   IntAct; P29457; 2.
DR   STRING; 10116.ENSRNOP00000022983; -.
DR   MEROPS; I04.035; -.
DR   GlyCosmos; P29457; 3 sites, No reported glycans.
DR   GlyGen; P29457; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P29457; -.
DR   PhosphoSitePlus; P29457; -.
DR   SwissPalm; P29457; -.
DR   PaxDb; 10116-ENSRNOP00000022983; -.
DR   GeneID; 29345; -.
DR   KEGG; rno:29345; -.
DR   UCSC; RGD:69302; rat.
DR   AGR; RGD:69302; -.
DR   CTD; 871; -.
DR   RGD; 69302; Serpinh1.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P29457; -.
DR   OMA; AAEAMWV; -.
DR   PhylomeDB; P29457; -.
DR   Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR   PRO; PR:P29457; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005518; F:collagen binding; TAS:RGD.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0003433; P:chondrocyte development involved in endochondral bone morphogenesis; ISO:RGD.
DR   GO; GO:0032964; P:collagen biosynthetic process; ISO:RGD.
DR   GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR   GO; GO:0051604; P:protein maturation; ISO:RGD.
DR   CDD; cd02046; serpinH1_CBP1; 1.
DR   FunFam; 3.30.497.10:FF:000047; Serpin H1; 1.
DR   FunFam; 2.30.39.10:FF:000072; Serpin peptidase inhibitor, clade H (Heat shock protein 47), member 1, (Collagen binding protein 1); 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   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   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; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Phosphoprotein; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:1654327,
FT                   ECO:0000269|PubMed:2158279"
FT   CHAIN           18..417
FT                   /note="Serpin H1"
FT                   /id="PRO_0000032518"
FT   MOTIF           414..417
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000305"
FT   SITE            376..377
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         93
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19324"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50454"
FT   MOD_RES         206
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19324"
FT   MOD_RES         295
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19324"
FT   MOD_RES         318
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19324"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  46518 MW;  859C4E16B15E7DC1 CRC64;
     MRSLLLGTLC LLAVALAAEV KKPVEAAAPG TAEKLSSKAT TLAERSTGLA FSLYQAMAKD
     QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK LRDEEVHTGL GELVRSLSNS
     TARNVTWKLG SRLYGPSSVS FADDFVRSSK QHYNCEHSKI NFRDKRSALQ SINEWASQTT
     DGKLPEVTKD VERTDGALLV NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG
     LYNYYDDEKE KLQLVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK TWMGKMQKKA
     VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV FHATAFEWDT
     EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL FIGRLVRPKG DKMRDEL
//