HP55_TAMSI
ID HP55_TAMSI Reviewed; 413 AA.
AC Q09055; O54756;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 4.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Hibernation-specific plasma protein HP-55;
DE AltName: Full=CM55-ML;
DE AltName: Full=Hibernator-specific blood complex, 55 kDa subunit;
DE Flags: Precursor;
OS Tamias sibiricus (Siberian chipmunk) (Eutamias sibiricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Tamias.
OX NCBI_TaxID=64680;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9434174; DOI=10.1016/s0378-1119(97)00532-5;
RA Takamatsu N., Kojima M., Taniyama M., Ohba K., Uematsu T., Segawa C.,
RA Tsutou S., Watanabe M., Kondo J., Kondo N., Shiba T.;
RT "Expression of multiple alpha1-antitrypsin-like genes in hibernating
RT species of the squirrel family.";
RL Gene 204:127-132(1997).
RN [2]
RP PROTEIN SEQUENCE OF 35-54; 89-126; 149-193; 279-292; 303-344; 356-375;
RP 385-399 AND 408-413, PYROGLUTAMATE FORMATION AT GLN-25, INTERACTION WITH
RP HP-20; HP-25 AND HP-27, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Plasma;
RX PubMed=1730610; DOI=10.1016/s0021-9258(18)48519-5;
RA Kondo N., Kondo J.;
RT "Identification of novel blood proteins specific for mammalian
RT hibernation.";
RL J. Biol. Chem. 267:473-478(1992).
CC -!- FUNCTION: Protease inhibitor. {ECO:0000250}.
CC -!- SUBUNIT: Plasma proteins HP-20, HP-25, HP-27 and HP-55 form a 140 kDa
CC complex via disulfide bonds in the plasma.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1730610}.
CC -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC {ECO:0000269|PubMed:1730610}.
CC -!- DEVELOPMENTAL STAGE: The protein complex disappears from the plasma at
CC onset of hibernation and reappears as hibernation ceases.
CC {ECO:0000269|PubMed:1730610}.
CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC protein and directs binding to the target protease. The protease
CC cleaves the serpin at the reactive site within the RCL, establishing a
CC covalent linkage between the serpin reactive site and the active site
CC of the protease. The resulting inactive serpin-protease complex is
CC highly stable (By similarity). {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AB000545; BAA24415.1; -; mRNA.
DR AlphaFoldDB; Q09055; -.
DR SMR; Q09055; -.
DR MEROPS; I04.001; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
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 PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hibernation;
KW Protease inhibitor; Pyrrolidone carboxylic acid; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..413
FT /note="Hibernation-specific plasma protein HP-55"
FT /id="PRO_0000032402"
FT REGION 368..387
FT /note="RCL"
FT SITE 377..378
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:1730610"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 115
FT /note="F -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="R -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="S -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45992 MW; F99B05F28B290429 CRC64;
MPSSISWGLL LLAALSCLGP GSLAQDAQET EASKQDQEHP ASHRIAPHLA EFALSLYRVL
ARQSNTTNIF FSPVSIASAL AMLSLGTKGD THTQILEGLD FNLTEMAEAD IHQGFQNLLQ
TLNRPNTQLQ LTSGNVLFIH QNLKLLDKFL ENIKSLYHSG AFPTNFTNTE EARQQINSYV
EQGTQGKIVE LVKELDRDTV LALVNYIFFK GKWLKPFNVK NIREEDFHVD EATTVRVPMM
YRVGMFPVHY CRTLASLVLQ MDYLGNATAI FLLPDKGKMQ HLEDTISTEI LSKLLKDRQT
SKYQVYFPRV SISGTYDLKD VLSSLGITRV FSRVADLSGV TEDAPLTVSK VLHKAVLDMD
EEGTEAAGGT VLGAEAMLQA PIMKFDRPFL VVIYEHNTKS PLFVGKVVNP TQQ
