P19324 (SERPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serpin H1

Alternative name(s):
47 kDa heat shock protein
Collagen-binding protein
Short name=Colligin
Serine protease inhibitor J6

Gene names

Name:	Serpinh1
Synonyms:	Cbp1, Hsp47

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
Subcellular location	Endoplasmic reticulum lumen.
Induction	By heat shock and retinoic acid.
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Chaperone
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	collagen biosynthetic process Inferred from mutant phenotype PubMed 10995453. Source: MGI collagen fibril organization Inferred from mutant phenotype PubMed 10995453. Source: MGI protein maturation Inferred from mutant phenotype PubMed 10995453. Source: MGI regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 8018053. Source: MGI endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: Compara
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome unfolded protein binding Inferred from direct assay PubMed 10862616. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Ref.1
	Chain	18 – 417	400	Serpin H1		PRO_0000032517
Regions
	Motif	414 – 417	4	Prevents secretion from ER Probable
Sites
	Site	376 – 377	2	Reactive bond homolog By similarity
Amino acid modifications
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	124	1	N-linked (GlcNAc...) Potential
	Glycosylation	394	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	176	1	A → P in AAA03200. Ref.2
	Sequence conflict	212	1	K → R in CAA43091. Ref.1
	Sequence conflict	212	1	K → R in AAA03200. Ref.2
	Sequence conflict	216	1	K → R in CAA43091. Ref.1
	Sequence conflict	216	1	K → R in AAA03200. Ref.2
	Sequence conflict	270 – 271	2	MP → IA in AAA03200. Ref.2
	Sequence conflict	277	1	L → S in AAA03200. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P19324 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 1124A050A6CC4F67	FASTA	417	46,534
	10 20 30 40 50 60 MRSLLLGTLC LLAVALAAEV KKPLEAAAPG TAEKLSSKAT TLAERSTGLA FSLYQAMAKD 70 80 90 100 110 120 QAVENILLSP LVVASSLGLV SLGGKATTAS QAKAVLSAEK LRDEEVHTGL GELLRSLSNS 130 140 150 160 170 180 TARNVTWKLG SRLYGPSSVS FADDFVRSSK QHYNCEHSKI NFRDKRSALQ SINEWASQTT 190 200 210 220 230 240 DGKLPEVTKD VERTDGALLV NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVTMMHRTG 250 260 270 280 290 300 LYNYYDDEKE KLQMVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK AWMGKMQKKA 310 320 330 340 350 360 VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV FHATAFEWDT 370 380 390 400 410 EGNPFDQDIY GREELRSPKL FYADHPFIFL VRDNQSGSLL FIGRLVRPKG DKMRDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells." Takechi H., Hirayoshi K., Nakai A., Kudo H., Saga S., Kita T., Nagata K. Eur. J. Biochem. 206:323-329(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-43. Strain: BALB/c.
[2]	"A retinoic acid-inducible mRNA from F9 teratocarcinoma cells encodes a novel protease inhibitor homologue." Wang S.-Y., Gudas L.J. J. Biol. Chem. 265:15818-15822(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Teratocarcinoma.
[3]	Erratum Wang S.-Y., Gudas L.J. J. Biol. Chem. 266:14135-14135(1991) [PubMed] [Europe PMC] [Abstract]
[4]	"Structure of the gene and its retinoic acid-regulatory region for murine J6 serpin. An F9 teratocarcinoma cell retinoic acid-inducible protein." Wang S.-Y. J. Biol. Chem. 267:15362-15366(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Structure of the gene encoding the mouse 47-kDa heat-shock protein (HSP47)." Hosokawa N., Takechi H., Yokota S.I., Hirayoshi K., Nagata K. Gene 126:187-193(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head, Heart, Skin, Stomach and Testis.
[7]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60676 mRNA. Translation: CAA43091.1. J05609 mRNA. Translation: AAA03200.1. Sequence problems. D12907 Genomic DNA. Translation: BAA02298.1. AK029080 mRNA. Translation: BAC26283.1. AK031457 mRNA. Translation: BAC27413.1. AK077660 mRNA. Translation: BAC36935.1. AK077937 mRNA. Translation: BAC37075.1. AK086519 mRNA. Translation: BAC39683.1. AK086523 mRNA. Translation: BAC39684.1. AK089993 mRNA. Translation: BAC41032.1. AK090103 mRNA. Translation: BAC41093.1. AK159998 mRNA. Translation: BAE35546.1. AK168442 mRNA. Translation: BAE40347.1. AK168870 mRNA. Translation: BAE40689.1. AC158748 Genomic DNA. No translation available. BC085143 mRNA. Translation: AAH85143.1.
IPI	IPI00114733.
PIR	A42843. S23453.
RefSeq	NP_001104513.1. NM_001111043.1. NP_001104514.1. NM_001111044.1. NP_033955.2. NM_009825.2.
UniGene	Mm.22708. Mm.444951.
3D structure databases
ProteinModelPortal	P19324.
SMR	P19324. Positions 35-417.
ModBase	Search...
Protein family/group databases
MEROPS	I04.035.
PTM databases
PhosphoSite	P19324.
2D gel databases
REPRODUCTION-2DPAGE	IPI00114733.
Proteomic databases
PaxDb	P19324.
PRIDE	P19324.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000094154; ENSMUSP00000091706; ENSMUSG00000070436. ENSMUST00000169437; ENSMUSP00000126390; ENSMUSG00000070436.
GeneID	12406.
KEGG	mmu:12406.
Organism-specific databases
CTD	871.
MGI	MGI:88283. Serpinh1.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00560000076649.
HOGENOM	HOG000238519.
HOVERGEN	HBG104930.
InParanoid	Q5U4D0.
KO	K09501.
OMA	INEWASQ.
OrthoDB	EOG43FGX2.
Gene expression databases
Bgee	P19324.
Genevestigator	P19324.
GermOnline	ENSMUSG00000070436. Mus musculus.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P19324.
ChEMBL	CHEMBL1163113.
ChiTaRS	SERPINH1. mouse.
NextBio	281182.
SOURCE	Search...

Entry information

Entry name

SERPH_MOUSE

Accession

Primary (citable) accession number: P19324
Secondary accession number(s): Q5U4D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program