SERPH_RAT
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 25-MAY-2022, entry version 141.
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_058869.1; NM_017173.1.
DR AlphaFoldDB; P29457; -.
DR SMR; P29457; -.
DR BioGRID; 248001; 2.
DR ELM; P29457; -.
DR IntAct; P29457; 1.
DR STRING; 10116.ENSRNOP00000022983; -.
DR MEROPS; I04.035; -.
DR GlyGen; P29457; 3 sites.
DR iPTMnet; P29457; -.
DR PhosphoSitePlus; P29457; -.
DR SwissPalm; P29457; -.
DR PaxDb; P29457; -.
DR PRIDE; P29457; -.
DR GeneID; 29345; -.
DR KEGG; rno:29345; -.
DR UCSC; RGD:69302; rat.
DR CTD; 871; -.
DR RGD; 69302; Serpinh1.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P29457; -.
DR OrthoDB; 1124079at2759; -.
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:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; TAS:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
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 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
