ID   HSP97_STRPU             Reviewed;         889 AA.
AC   Q06068; Q94761;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=97 kDa heat shock protein;
DE   AltName: Full=Egg sperm receptor;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 154-169 AND 481-495.
RC   TISSUE=Ovary;
RX   PubMed=8383878; DOI=10.1126/science.8383878;
RA   Foltz K.R., Partin J.S., Lennarz W.J.;
RT   "Sea urchin egg receptor for sperm: sequence similarity of binding domain
RT   and hsp70.";
RL   Science 259:1421-1425(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Lennarz W.J.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface recognition protein that binds acrosome-reacted
CC       sperm and thereby mediates binding and subsequent fusion of the sperm
CC       and egg.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:8383878) thought to have a N-terminal
CC       sequence signal and a C-terminal transmembrane region. Both domains do
CC       not exist in the revised sequence. {ECO:0000305|PubMed:8383878}.
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DR   EMBL; L04969; AAB09737.1; -; mRNA.
DR   PIR; T11742; T11742.
DR   AlphaFoldDB; Q06068; -.
DR   SMR; Q06068; -.
DR   STRING; 7668.SPU_002779-tr; -.
DR   PRIDE; Q06068; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   HOGENOM; CLU_005965_5_1_1; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 2.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..889
FT                   /note="97 kDa heat shock protein"
FT                   /id="PRO_0000078673"
FT   REGION          504..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..838
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  98619 MW;  1520EEDF70B0E0CF CRC64;
     MSVVGFDVGN LSSYIAVARG GGIETMANEY SDRLTPSVVS FGEKSRTQGH AARSQAITNY
     KNTLSQFKRF IARRFSDPSV QKDAKVVPYK ITQLPNGNVG MQVQYLGETE TFTPEQIYAM
     ILTKLKSTAE INLCRKVVDC VISVPQYYTD LERRGVIHAA EIAGLNCLRV ISDTTAVALA
     YGIYKQDLPT PEEKPRNVVF VDCGHSSLQV SVCAFNKGKL KVLANASDKN LGGRDFDWLL
     AEHFAVDFQT RYKMDVKSNQ RAWLRLMAEC DKTKKLMSAN ATLISMNIEC IMNDRDVSGK
     ISRADFEALA AELLKRVEVP LKSVLEQTKL KPEDIHSIEI VGGSSRIPSI KETIKKVFKK
     ECSTTLNQDE AVARGCALQC AILSPTFKVR DFTVTDLTPY PIELEWKGTE GEDGSMEVSS
     KNHQAPFSKM LTFYRKAPFE LVARYADPNL PIPERRIGRF KINGVFPTTE GESSKIKVKV
     RVDGHGIFNV ASASLIEKLP VQAEDAMEDG SPEENGPSKE EGSGASQAEN DAPMDQSPVQ
     GGAGEGEASA DKEEQADNGS KETSKDSKDQ TSESSKSDKE SKDQNSEGSK SDNSSTETDA
     KAAKKTKKTI KTHELSITAT TDELSITEVN NFFEKEGKLI AHDRLEKEKN DAKNAVEEYV
     YEMREKLCDK FEQYISEKER GSFSKLLEET ENWLYEDGED ETKSVYQTKI NSLKKIGDPV
     ENRFKENLER PGAFEDFGKA LVPYIKTLDL YSNGDEKYSH IEKEDMAKVE KCVKEKVAWR
     DSKVNAQNQK APHQDPVVTA AQIRSEIQSM KFVCDPIINK PKPKPKEEPP KDNGPTPEEA
     AKDGGPAPPT TEGGEEKMDT SDQAPTGEAS KEGETKPDET KPDVEMELD