ID   HS7EB_XENLA             Reviewed;         507 AA.
AC   A2VD93;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Heat shock 70 kDa protein 14-B;
GN   Name=hspa14-b;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Intestine;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ribosome-associated complex (RAC), a complex
CC       involved in folding or maintaining nascent polypeptides in a folding-
CC       competent state. {ECO:0000250}.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BC129620; AAI29621.1; -; mRNA.
DR   RefSeq; NP_001091353.1; NM_001097884.1.
DR   AlphaFoldDB; A2VD93; -.
DR   SMR; A2VD93; -.
DR   DNASU; 100037193; -.
DR   GeneID; 100037193; -.
DR   KEGG; xla:100037193; -.
DR   CTD; 100037193; -.
DR   Xenbase; XB-GENE-17342099; hspa14.S.
DR   OrthoDB; 646813at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 100037193; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10238; HSPA14-like_NBD; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042049; HSPA14_NBD.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Heat shock 70 kDa protein 14-B"
FT                   /id="PRO_0000405829"
SQ   SEQUENCE   507 AA;  54290 MW;  FA99A83B22ADD310 CRC64;
     MAAIGVHLGC TCACVAVFKD GRADVVANDA GDRVTPAVVG FLEKEVIVGL AAKQSRVRNA
     TNTIVKVKQI LGRSYGDPIA QKHITESKCT VVEKGGKPKY EIDTGETQKL VSSEDVAKLI
     FSKMKETAQS ALGSDVNDVV ITVPFDFGES QKKALGEAAS AAGFNILRMI HEPSAALLAY
     GIGQESPTGK SNVLVYKLGG TSLSVTMIEV NSGIYRVLAT STYDGIGGVC FTEALAQHLA
     SEFQRTYKQD IRGNARAMMK LMNSADVAKH ALSTLGSSNC FVDSLYDGID FDCSVSRARF
     ELICSSLFNQ CIDPIKKLLE QVGFKATDVN QVVLCGGSAR IPKLQQLIKD LFPEVEMLSS
     IPPDEVIPVG AAIQAGILLG KENTDLDTIT IECSASDMLV KEIDESGNKF TVLLPSGTPL
     PARRQHVLQA PGNISSVCLE LYESDGKSSV SEECKFAQVV LKDLQKKTSG VRDILTVLTM
     KRDGSLHITC TDKDSGKSEM ITIEDTS