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   24-JAN-2024, entry version 116.
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.ENSBTAP00000072322; -.
DR   MEROPS; I04.035; -.
DR   GlyCosmos; Q2KJH6; 2 sites, No reported glycans.
DR   SwissPalm; Q2KJH6; -.
DR   PaxDb; 9913-ENSBTAP00000039506; -.
DR   PeptideAtlas; Q2KJH6; -.
DR   Ensembl; ENSBTAT00000039717.3; ENSBTAP00000039506.2; ENSBTAG00000001027.4.
DR   Ensembl; ENSBTAT00000083385.1; ENSBTAP00000072322.1; ENSBTAG00000001027.4.
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; 3218836at2759; -.
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 cell types or 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:0051604; P:protein maturation; IEA:Ensembl.
DR   CDD; cd02046; serpinH1_CBP1; 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   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
//