SERPH_MOUSE
ID SERPH_MOUSE Reviewed; 417 AA.
AC P19324; Q5U4D0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 188.
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=Serine protease inhibitor J6;
DE Flags: Precursor;
GN Name=Serpinh1; Synonyms=Cbp1, Hsp47;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-43.
RC STRAIN=BALB/cJ;
RX PubMed=1317794; DOI=10.1111/j.1432-1033.1992.tb16930.x;
RA Takechi H., Hirayoshi K., Nakai A., Kudo H., Saga S., Kita T., Nagata K.;
RT "Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a
RT collagen-binding stress protein, and its expression during the
RT differentiation of F9 teratocarcinoma cells.";
RL Eur. J. Biochem. 206:323-329(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=2394749; DOI=10.1016/s0021-9258(18)55471-5;
RA Wang S.-Y., Gudas L.J.;
RT "A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a
RT novel protease inhibitor homologue.";
RL J. Biol. Chem. 265:15818-15822(1990).
RN [3]
RP ERRATUM OF PUBMED:2394749.
RX PubMed=1856236; DOI=10.1016/s0021-9258(18)92819-x;
RA Wang S.-Y., Gudas L.J.;
RL J. Biol. Chem. 266:14135-14135(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1639782; DOI=10.1016/s0021-9258(19)49542-2;
RA Wang S.-Y.;
RT "Structure of the gene and its retinoic acid-regulatory region for murine
RT J6 serpin. An F9 teratocarcinoma cell retinoic acid-inducible protein.";
RL J. Biol. Chem. 267:15362-15366(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8482533; DOI=10.1016/0378-1119(93)90366-b;
RA Hosokawa N., Takechi H., Yokota S.I., Hirayoshi K., Nagata K.;
RT "Structure of the gene encoding the mouse 47-kDa heat-shock protein
RT (HSP47).";
RL Gene 126:187-193(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Heart, Skin, Stomach, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-318, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-93 AND LYS-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X60676; CAA43091.1; -; mRNA.
DR EMBL; J05609; AAA03200.1; ALT_SEQ; mRNA.
DR EMBL; D12907; BAA02298.1; -; Genomic_DNA.
DR EMBL; AK029080; BAC26283.1; -; mRNA.
DR EMBL; AK031457; BAC27413.1; -; mRNA.
DR EMBL; AK077660; BAC36935.1; -; mRNA.
DR EMBL; AK077937; BAC37075.1; -; mRNA.
DR EMBL; AK086519; BAC39683.1; -; mRNA.
DR EMBL; AK086523; BAC39684.1; -; mRNA.
DR EMBL; AK089993; BAC41032.1; -; mRNA.
DR EMBL; AK090103; BAC41093.1; -; mRNA.
DR EMBL; AK159998; BAE35546.1; -; mRNA.
DR EMBL; AK168442; BAE40347.1; -; mRNA.
DR EMBL; AK168870; BAE40689.1; -; mRNA.
DR EMBL; AC158748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC085143; AAH85143.1; -; mRNA.
DR CCDS; CCDS21480.1; -.
DR PIR; S23453; A42843.
DR RefSeq; NP_001104513.1; NM_001111043.1.
DR RefSeq; NP_001104514.1; NM_001111044.1.
DR RefSeq; NP_001272705.1; NM_001285776.1.
DR RefSeq; NP_033955.2; NM_009825.2.
DR RefSeq; XP_006507341.1; XM_006507278.3.
DR RefSeq; XP_006507342.1; XM_006507279.3.
DR AlphaFoldDB; P19324; -.
DR SMR; P19324; -.
DR BioGRID; 198530; 16.
DR CORUM; P19324; -.
DR IntAct; P19324; 2.
DR MINT; P19324; -.
DR STRING; 10090.ENSMUSP00000126390; -.
DR BindingDB; P19324; -.
DR ChEMBL; CHEMBL1163113; -.
DR MEROPS; I04.035; -.
DR GlyConnect; 2705; 4 N-Linked glycans (1 site).
DR GlyGen; P19324; 3 sites, 4 N-linked glycans (1 site).
DR iPTMnet; P19324; -.
DR PhosphoSitePlus; P19324; -.
DR SwissPalm; P19324; -.
DR REPRODUCTION-2DPAGE; IPI00114733; -.
DR jPOST; P19324; -.
DR MaxQB; P19324; -.
DR PaxDb; P19324; -.
DR PeptideAtlas; P19324; -.
DR PRIDE; P19324; -.
DR ProteomicsDB; 255391; -.
DR TopDownProteomics; P19324; -.
DR Antibodypedia; 3838; 532 antibodies from 36 providers.
DR DNASU; 12406; -.
DR Ensembl; ENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436.
DR Ensembl; ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
DR Ensembl; ENSMUST00000207849; ENSMUSP00000147064; ENSMUSG00000070436.
DR Ensembl; ENSMUST00000208119; ENSMUSP00000146969; ENSMUSG00000070436.
DR GeneID; 12406; -.
DR KEGG; mmu:12406; -.
DR UCSC; uc009ilj.2; mouse.
DR CTD; 871; -.
DR MGI; MGI:88283; Serpinh1.
DR VEuPathDB; HostDB:ENSMUSG00000070436; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000156163; -.
DR HOGENOM; CLU_023330_2_0_1; -.
DR InParanoid; P19324; -.
DR OMA; WDEKFHE; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P19324; -.
DR TreeFam; TF343094; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 12406; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Serpinh1; mouse.
DR PRO; PR:P19324; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P19324; protein.
DR Bgee; ENSMUSG00000070436; Expressed in humerus cartilage element and 261 other tissues.
DR ExpressionAtlas; P19324; baseline and differential.
DR Genevisible; P19324; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
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:0051082; F:unfolded protein binding; IDA:MGI.
DR GO; GO:0003433; P:chondrocyte development involved in endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:0032964; P:collagen biosynthetic process; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IMP:MGI.
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:1317794"
FT CHAIN 18..417
FT /note="Serpin H1"
FT /id="PRO_0000032517"
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:0007744|PubMed:23806337"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50454"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 295
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
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"
FT CONFLICT 176
FT /note="A -> P (in Ref. 2; AAA03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="K -> R (in Ref. 1; CAA43091 and 2; AAA03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="K -> R (in Ref. 1; CAA43091 and 2; AAA03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..271
FT /note="MP -> IA (in Ref. 2; AAA03200)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> S (in Ref. 2; AAA03200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46534 MW; 1124A050A6CC4F67 CRC64;
MRSLLLGTLC LLAVALAAEV KKPLEAAAPG TAEKLSSKAT TLAERSTGLA FSLYQAMAKD
QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK LRDEEVHTGL GELLRSLSNS
TARNVTWKLG SRLYGPSSVS FADDFVRSSK QHYNCEHSKI NFRDKRSALQ SINEWASQTT
DGKLPEVTKD VERTDGALLV NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG
LYNYYDDEKE KLQMVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK AWMGKMQKKA
VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV FHATAFEWDT
EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL FIGRLVRPKG DKMRDEL
