SERPH_BOVIN
ID SERPH_BOVIN Reviewed; 418 AA.
AC Q2KJH6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serpin H1;
DE AltName: Full=Collagen-binding protein;
DE Short=Colligin;
DE Flags: Precursor;
GN Name=SERPINH1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds specifically to collagen. Could be involved as a
CC chaperone in the biosynthetic pathway of collagen (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; BC105338; AAI05339.1; -; mRNA.
DR RefSeq; NP_001039528.1; NM_001046063.1.
DR RefSeq; XP_005216304.1; XM_005216247.2.
DR RefSeq; XP_005216305.1; XM_005216248.3.
DR AlphaFoldDB; Q2KJH6; -.
DR SMR; Q2KJH6; -.
DR STRING; 9913.ENSBTAP00000039506; -.
DR MEROPS; I04.035; -.
DR PaxDb; Q2KJH6; -.
DR PeptideAtlas; Q2KJH6; -.
DR PRIDE; Q2KJH6; -.
DR Ensembl; ENSBTAT00000039717; ENSBTAP00000039506; ENSBTAG00000001027.
DR Ensembl; ENSBTAT00000083385; ENSBTAP00000072322; ENSBTAG00000001027.
DR GeneID; 510850; -.
DR KEGG; bta:510850; -.
DR CTD; 871; -.
DR VEuPathDB; HostDB:ENSBTAG00000001027; -.
DR VGNC; VGNC:34480; SERPINH1.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000156163; -.
DR HOGENOM; CLU_023330_2_0_1; -.
DR InParanoid; Q2KJH6; -.
DR OMA; WDEKFHE; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF343094; -.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000001027; Expressed in diaphragm and 104 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:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0003433; P:chondrocyte development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
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 GO; GO:0051604; P:protein maturation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..418
FT /note="Serpin H1"
FT /id="PRO_0000253604"
FT MOTIF 415..418
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT SITE 377..378
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19324"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50454"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19324"
FT MOD_RES 296
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19324"
FT MOD_RES 319
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19324"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 418 AA; 46507 MW; DE81C53C711EF152 CRC64;
MRALLLISTI CLLARALAAE VKKPAAAAAP GTAEKLSPKA ATLAERSAGL AFSLYQAMAK
DQAVENILLS PVVVASSLGL VSLGGKAATA SQAKAVLSAE QLRDDEVHAG LGELLRSLSN
STARNVTWKL GSRLYGPSSV SFAEDFVRSS KQHYNCEHSK INFRDKRSAL QSINEWAAQT
TDGKLPEVTK DVERTDGALL VNAMFFKPHW DERFHHKMVD NRGFMVTRSY TVGVTMMHRT
GLYNYYDDEK EKLQMVEMPL AHKLSSLIII MPHHVEPLER LEKLLTKEQL KVWMGKMQKK
AVAISLPKGV VEVTHDLQKH LAGLGLTEAI DKNKADLSRM SGKKDLYLAS VFHATAFEWD
TDGNPFDQDI YGREELRSPK LFYADHPFIF LVRDTQSGSL LFIGRLVRPK GDKMRDEL
