ID   A0A3B4VC66_SERDU        Unreviewed;       410 AA.
AC   A0A3B4VC66;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Serpin H1 {ECO:0000256|ARBA:ARBA00013551};
DE   AltName: Full=Collagen-binding protein {ECO:0000256|ARBA:ARBA00030441};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000027535.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000027535.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Binds specifically to collagen. Could be involved as a
CC       chaperone in the biosynthetic pathway of collagen.
CC       {ECO:0000256|ARBA:ARBA00025405}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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   AlphaFoldDB; A0A3B4VC66; -.
DR   Ensembl; ENSSDUT00000028019.1; ENSSDUP00000027535.1; ENSSDUG00000019915.1.
DR   GeneTree; ENSGT00940000156163; -.
DR   OMA; EMDTSIF; -.
DR   OrthoDB; 3218836at2759; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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; 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; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..410
FT                   /note="Serpin H1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017420845"
FT   DOMAIN          44..401
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   410 AA;  45494 MW;  517075DD73DD6630 CRC64;
     MWVTNLVALA LLATSASAAT SASADKVLSN HATILADNSA NLAFTLYQNM AKEKNIENIL
     ISPVVVASSL GLVALGGKAS TASQVKTILN AAKVKDEQLH SGLAELLTEV SDPKTRNVTW
     KISNRLYGPN SVNFVDDFVK SSKKHYNCDQ SKINFKDKKS AVNSINEWAA KSTGGKLPEV
     TKDVAKTDGA MIVNAMFFKP HWDEQFHHQM VDNRGFMVSR SYTVSVQMMH RTGLYGFYDD
     STNKLSILSM PLAHKKSSVV FIMPYHLEPL ERLEKILTKK QLDTWMGKLQ EKAVAVSLPK
     VSMEVSHDLQ KHLGELGLTE AVDKSKADFS KISGKKDLYL SSVFHASAME WDTAGNEIDT
     SIFGTDKLKS PKLFYADHPF IFLVKDQKTN SILFIGRMVR PKGEKMRDEL
//