SHR2_STRPU
ID SHR2_STRPU Reviewed; 583 AA.
AC Q26622; Q26624; Q26625; Q7JPB0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Orphan steroid hormone receptor 2;
DE AltName: Full=SpSHR2;
GN Name=SHR2 {ECO:0000303|PubMed:8806817};
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] {ECO:0000305, ECO:0000312|EMBL:AAB19174.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 16-153, DNA-BINDING, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:8806817};
RX PubMed=8806817; DOI=10.1006/dbio.1996.0171;
RA Kontrogianni-Konstantopoulos A., Vlahou A., Vu D., Flytzanis C.N.;
RT "A novel sea urchin nuclear receptor encoded by alternatively spliced
RT maternal RNAs.";
RL Dev. Biol. 177:371-382(1996).
RN [2] {ECO:0000305}
RP DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9664037; DOI=10.1242/jcs.111.15.2159;
RA Kontrogianni-Konstantopoulos A., Leahy P.S., Flytzanis C.N.;
RT "Embryonic and post-embryonic utilization and subcellular localization of
RT the nuclear receptor SpSHR2 in the sea urchin.";
RL J. Cell Sci. 111:2159-2169(1998).
RN [3] {ECO:0000305}
RP DNA-BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11553912; DOI=10.1002/mrd.1071;
RA Kontrogianni-Konstantopoulos A., Flytzanis C.N.;
RT "Differential cellular compartmentalization of the nuclear receptor SpSHR2
RT splicing variants in early sea urchin embryos.";
RL Mol. Reprod. Dev. 60:147-157(2001).
CC -!- FUNCTION: Orphan nuclear receptor. Binds to the hormone response
CC element in the upstream promoter region of the CYIIIB gene in vitro.
CC Both isoform 1 and isoform 2 bind DNA. {ECO:0000269|PubMed:11553912,
CC ECO:0000269|PubMed:8806817, ECO:0000269|PubMed:9664037}.
CC -!- SUBUNIT: Binds DNA as a monomer. {ECO:0000269|PubMed:11553912}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The subcellular location
CC of isoform 1 alters throughout development. In the unfertilized egg,
CC isoform 1 expression is cytoplasmic and concentrated around the
CC pronucleus. Following fertilization, the cytoplasmic protein rapidly
CC enters the embryonic nuclei where it appears as speckles. From the
CC fourth cleavage stage onwards it resides as speckles in the cytoplasm
CC and the nucleus. The cytoplasmic localization also differs between
CC cells, maintaining an apical position in polarized ectodermal and
CC endodermal cells, whereas in non-polarized cells the cytoplasmic
CC distribution is uniform. In contrast, isoform 2 resides in the nucleus
CC in both 4-cell and 16-cell embryos.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:8806817};
CC IsoId=Q26622-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8806817};
CC IsoId=Q26622-2; Sequence=VSP_051753;
CC -!- TISSUE SPECIFICITY: Expressed uniformly in the early embryo. In
CC contrast, larval expression is localized to the epaulettes and mouth
CC epithelium. Expressed in multiple adult organs including lantern
CC muscle, tubefeet, intestine, coelomocytes and gonads. In the adult
CC ovaries and testes, expression is specifically localized to the smooth
CC muscle epithelial layer of cells which surround the ovarioles and
CC acini, respectively (at protein level). {ECO:0000269|PubMed:9664037}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Present
CC in the unfertilized egg and in all embryonic stages up to the pluteus
CC stage, followed by depletion of expression in the late embryo.
CC Expression starts again just prior to metamorphosis in larva at 35 days
CC post-fertilization (dpf). Also expressed in adults (at protein level).
CC {ECO:0000269|PubMed:8806817, ECO:0000269|PubMed:9664037}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping.
CC {ECO:0000303|PubMed:8806817}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000255}.
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DR EMBL; U38281; AAB19174.1; -; mRNA.
DR EMBL; U38528; AAB19175.1; -; mRNA.
DR EMBL; U38529; AAB19176.1; -; Genomic_DNA.
DR RefSeq; NP_001116968.1; NM_001123496.1. [Q26622-1]
DR AlphaFoldDB; Q26622; -.
DR STRING; 7668.SPU_008117-tr; -.
DR EnsemblMetazoa; NM_001123496; NP_001116968; GeneID_373398. [Q26622-1]
DR GeneID; 373398; -.
DR KEGG; spu:373398; -.
DR CTD; 373398; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_16_2_1; -.
DR InParanoid; Q26622; -.
DR OMA; DIQPEDQ; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..583
FT /note="Orphan steroid hormone receptor 2"
FT /id="PRO_0000053754"
FT DOMAIN 248..563
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 84..159
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 87..107
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 123..142
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT VAR_SEQ 176..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8806817"
FT /id="VSP_051753"
SQ SEQUENCE 583 AA; 63853 MW; DCB79BF48B89B833 CRC64;
MGMVSSQATP VEAYKVQQVQ INDQTVEQLV RVQTSAGTTV TTIDAATAER LVKLREEDLI
KFSAQGMSQA QMMAKPGMTS PRPIELCAVC GDKASGRHYG AISCEGCKGF FKRSIRKHLG
YTCRGNKDCQ IIKHNRNRCQ YCRLQKCLDM GMKSDSVQCE RSPLKTRDKT PGNCAASTDK
IYIRKDIRSP LTATPTFVTG SVLAGGDMKS PQGNRQGLFD QGILLNVQTT PTSSPSASTS
DSTTDLSTLA SVVTSLANMN KKTEEGPSHS QQIYSPSQTL QIISNGDQDV QGGGDNVSKA
FDALTKALNT SGDSEAGDLS IDQSANGGSS EVELVKLDSP MLSDHHMQFK LTTPSPMPQF
LNVHYICESA SRLLFLSMHW ARSLPAFQVL SADTHTSMVQ KCWSELFTLG LAQCAQAMAL
STILTAIVNH LQTSLQQDKL SADRVKAVME HIWKLQEFVT TTSKLDVDQT EFAYLKTIVL
FSPDHPGLSN VRQIEKFQEM AISELHDYEA QTYPSKLNRF SKLLLRLPTL RLLSPAIMEE
LFFAGLIGNV QIDSIIPYIL RMETADYNSA QITMSASPGS LIG
