HGV2_HALRO
ID HGV2_HALRO Reviewed; 510 AA.
AC Q02508;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Protein HGV2;
GN Name=HGV2;
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=8468323; DOI=10.1093/oxfordjournals.jbchem.a124024;
RA Fujiwara S., Kawahara H., Makabe K.W., Satoh N.;
RT "A complementary DNA for an ascidian embryonic nuclear antigen Hgv2 encodes
RT a protein closely related to the amphibian histone-binding protein N1.";
RL J. Biochem. 113:189-195(1993).
CC -!- FUNCTION: May function as a nucleosome assembly factor during rapid
CC embryonic cell divisions.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Embryo and larvae.
CC -!- DEVELOPMENTAL STAGE: This protein is detected in the nuclei of all
CC cells in embryos and larvae but is not detected in the cells of
CC metamorphosed juveniles.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; D13541; BAA02741.1; -; mRNA.
DR PIR; JX0254; JX0254.
DR AlphaFoldDB; Q02508; -.
DR SMR; Q02508; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Nucleus; Repeat; TPR repeat.
FT CHAIN 1..510
FT /note="Protein HGV2"
FT /id="PRO_0000083967"
FT REPEAT 260..293
FT /note="TPR 1"
FT REPEAT 302..335
FT /note="TPR 2"
FT REGION 95..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 444..451
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 465..471
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 108..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 56872 MW; D9961E5953E976FF CRC64;
MVQDTEVVEA GTSKETETTV DVEKEIQECM GAGKKDLLCN DYSEAVNCFQ EACTLLSGKH
GQMAEECCEA YYYYGVSLLE LARLENGVLG NALKGVPEED ADGDSDQEQE QFEKPDLPET
EREKLREEVE AAMATEDEDT QEERGCPRRV EKKKEDDKPK ESEKSAEKSD EKEKEEKQAK
VESSTVKDVK DEKSSDKPVE SSNTEEPGTS GTSASSSKEN ESEEDPDDIS NMQLAWEMLE
LAKVLYKKHD KSKTNKQMVA QCHLKLGELG LEVENHPQAI GDFLECLVIQ KDLLPETDRK
LAETYYNLGL AYSFEKRYDN ALEHYQSALD VLEARVDMLN ELIESNEGNK EKEKEIISEC
KEVGELKELI PDINSKIEDV ILAKKQMQKL DGSPFRQASE GESSSGLGAS TSDDKPCSTI
PIRKVAPTSV PVAKDSPSDI THLVRRKRPS PDEDNQPAES KENESKKAKQ EETEEATNGH
SAVKKDTDVT DKNGTNGHSK TPKKDAAKRR