ID   HP27_TAMSI              Reviewed;         215 AA.
AC   Q06577;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Hibernation-associated plasma protein HP-27;
DE   AltName: Full=Hibernator-specific blood complex 27 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=8441393; DOI=10.1128/mcb.13.3.1516-1521.1993;
RA   Takamatsu N., Ohba K., Kondo J., Kondo N., Shiba T.;
RT   "Hibernation-associated gene regulation of plasma proteins with a collagen-
RT   like domain in mammalian hibernators.";
RL   Mol. Cell. Biol. 13:1516-1521(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 31-215.
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: Plasma proteins HP-20, HP-25, HP-27 and HP-55 form a 140 kDa
CC       complex via disulfide bonds in the plasma and are hibernation specific.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- DEVELOPMENTAL STAGE: The protein complex disappears from the plasma at
CC       onset of hibernation and reappears as hibernation ceases.
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DR   EMBL; D12976; BAA02353.1; -; mRNA.
DR   PIR; C48150; C48150.
DR   AlphaFoldDB; Q06577; -.
DR   SMR; Q06577; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Glycoprotein; Hibernation; Secreted;
KW   Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:1730610"
FT   CHAIN           31..215
FT                   /note="Hibernation-associated plasma protein HP-27"
FT                   /id="PRO_0000003560"
FT   DOMAIN          43..81
FT                   /note="Collagen-like"
FT   DOMAIN          85..215
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          34..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..79
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        41
FT                   /note="V -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="R -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  22797 MW;  D2357086A088FA9E CRC64;
     MYEAGKRASF MGGAGIWILA LSVLMHVVCS ETQGNPESCN VPGPQGPPGM RGPPGTPGKP
     GPPGWNGFPG LPGPPGPPGM TVNCHSKGTS AFAVKANELP PAPSQPVIFK EALHDAQGHF
     DLATGVFTCP VPGLYQFGFH IEAVQRAVKV SLMRNGTQVM EREAEAQDGY EHISGTAILQ
     LGMEDRVWLE NKLSQTDLER GTVQAVFSGF LIHEN