ID   SERPH_PONAB             Reviewed;         417 AA.
AC   Q5RBS3;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Serpin H1;
DE   AltName: Full=Collagen-binding protein;
DE            Short=Colligin;
DE   Flags: Precursor;
GN   Name=SERPINH1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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; CR858522; CAH90749.1; -; mRNA.
DR   EMBL; CR858561; CAH90787.1; -; mRNA.
DR   RefSeq; NP_001125445.1; NM_001131973.1.
DR   AlphaFoldDB; Q5RBS3; -.
DR   SMR; Q5RBS3; -.
DR   STRING; 9601.ENSPPYP00000004218; -.
DR   MEROPS; I04.035; -.
DR   GeneID; 100172353; -.
DR   KEGG; pon:100172353; -.
DR   CTD; 871; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q5RBS3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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; 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..417
FT                   /note="Serpin H1"
FT                   /id="PRO_0000253605"
FT   MOTIF           414..417
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   SITE            376..377
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         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        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   417 AA;  45762 MW;  BF7BA00DAC59FEC1 CRC64;
     MRSLLLLSAF CLLEAALAAE VKKPAAAAAP GTAEKLSPKA ATLAERSAGL AFSLYQAMAK
     DQAVENILVS PVVVASSLGL VSLGGKATTA SQAKAVLSAE QLRDEEVHAG LGELLRSLSN
     STARNVTWKL GSRLYGPSSV SFADDFVRTA SSTTTASTPR STSATSAALQ SINEWAAQTT
     DGKLPEVTKD VERTDGALLV NAMFFKPHWD EKFHHKMVDN RGFMVTRSYT VGVMMMHRTG
     LYNYYDDEKE KLQIVEMPLA HKLSSLIILM PHHVEPLERL EKLLTKEQLK IWMGKMQKKA
     VAISLPKGVV EVTHDLQKHL AGLGLTEAID KNKADLSRMS GKKDLYLASV FHATAFELDT
     DGNPFDQDIY GREELRSPKL FYADHPFIFL VRDTQSGSLL FIGRLVRPKG DKMRDEL