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 22-FEB-2023, entry version 94.
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 PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR PANTHER; PTHR15427:SF34; PROTEIN HP-25 HOMOLOG 2; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; TNF-like; 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
//
