ID Q6GMF1_XENLA Unreviewed; 634 AA.
AC Q6GMF1;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Heat shock protein family A (Hsp70) member 2 L homeolog {ECO:0000313|RefSeq:NP_001086039.1};
DE SubName: Full=MGC81782 protein {ECO:0000313|EMBL:AAH74113.1};
GN Name=hspa2.L {ECO:0000313|RefSeq:NP_001086039.1,
GN ECO:0000313|Xenbase:XB-GENE-992126};
GN Synonyms=hspa2 {ECO:0000313|RefSeq:NP_001086039.1,
GN ECO:0000313|Xenbase:XB-GENE-992126}, MGC81782
GN {ECO:0000313|EMBL:AAH74113.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH74113.1};
RN [1] {ECO:0000313|RefSeq:NP_001086039.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH74113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH74113.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001086039.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; BC074113; AAH74113.1; -; mRNA.
DR RefSeq; NP_001086039.1; NM_001092570.1.
DR DNASU; 444468; -.
DR GeneID; 444468; -.
DR KEGG; xla:444468; -.
DR AGR; Xenbase:XB-GENE-992126; -.
DR CTD; 444468; -.
DR Xenbase; XB-GENE-992126; hspa2.L.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 444468; Expressed in zone of skin and 18 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF382; HEAT SHOCK-RELATED 70 KDA PROTEIN 2; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Stress response {ECO:0000313|RefSeq:NP_001086039.1}.
FT REGION 615..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 69561 MW; 426DB114AFA44AB9 CRC64;
MSAKAPAVGI DLGTTYSCVG VFQHGKVEII ANEQGNRTTP SYVAFTDTER LIGDAARNQV
ALNPTNTIFD AKRLIGRRFD DPTVQSDMKH WPFTVVSDGG KPKVKVEYKG EAKTFFPEEI
SSMVLIKMKE VAEAYLGAKV PDAVITVPAY FNDSQRQATK DAGIIAGINV LRIINEPTAA
AIAYGLDKKS AGLGETNVLI FDLGGGTFDV SVLTIDGGIF EVKSTAGDTH LGGEDFDNRM
VAHFLDEFKR KNKKDISGNK RAVRRLRTAC ERAKRTLSSS TQASLEIDSL YEGTDFYTSI
TRARFEELCA DLFRGTLEPV EKALRDAKLD KGHIREIVLV GGSIRIPKIQ KLLQDFFNGR
ELNKSINPDE AVAYGAAVQA AILSGDKSHN VQDLLLLDVA PLSLGIETAG GVMTPLIKRN
TTIPSKQTQT FTTYSDNQSS VLVQVYEGER AMTRDNNLLG KFDLTGIPPA PRGVPQIEVT
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKEDIER MVNDADKYKA EDEVNRERVA
AKNGLESYTY HVKQTAEDEK LKGKLSEKEK SQILDKCKEV IDWLDKNQMA EKDEFEHKQK
ELEKVCNPII TKLYQGGAPN PGTAAGGPTI EEVD
//
