HER1_CAEEL
ID HER1_CAEEL Reviewed; 175 AA.
AC P34704;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein her-1;
DE AltName: Full=Hermaphrodization of XO animals protein 1;
DE Flags: Precursor;
GN Name=her-1; ORFNames=ZK287.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=Bristol N2;
RX PubMed=8436294; DOI=10.1101/gad.7.2.216;
RA Perry M.D., Li W., Trent C., Robertson B., Fire A., Hageman J.M.,
RA Wood W.B.;
RT "Molecular characterization of the her-1 gene suggests a direct role in
RT cell signaling during Caenorhabditis elegans sex determination.";
RL Genes Dev. 7:216-228(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 19-375.
RX PubMed=15289613; DOI=10.1073/pnas.0402559101;
RA Hamaoka B.Y., Dann C.E. III, Geisbrecht B.V., Leahy D.J.;
RT "Crystal structure of Caenorhabditis elegans HER-1 and characterization of
RT the interaction between HER-1 and TRA-2A.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11673-11678(2004).
CC -!- FUNCTION: Dictates male development. Probably plays a direct role in
CC cell signaling during C.elegans sex determination. Inhibits the
CC function of tra-2a.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P34704-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P34704-2; Sequence=VSP_004283;
CC -!- MISCELLANEOUS: [Isoform Long]: Active.
CC -!- MISCELLANEOUS: [Isoform Short]: Inactive. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z19595; CAA79650.1; -; Genomic_DNA.
DR EMBL; Z19595; CAA79651.1; -; Genomic_DNA.
DR EMBL; Z70757; CAA94804.1; -; Genomic_DNA.
DR PIR; A46388; A46388.
DR RefSeq; NP_001024310.1; NM_001029139.1. [P34704-1]
DR RefSeq; NP_001024311.2; NM_001029140.2. [P34704-2]
DR PDB; 1SZH; X-ray; 1.50 A; A/B=19-175.
DR PDBsum; 1SZH; -.
DR AlphaFoldDB; P34704; -.
DR SMR; P34704; -.
DR BioGRID; 44396; 44.
DR DIP; DIP-26672N; -.
DR STRING; 6239.ZK287.8a; -.
DR PaxDb; P34704; -.
DR EnsemblMetazoa; ZK287.8a.1; ZK287.8a.1; WBGene00001842. [P34704-1]
DR GeneID; 179360; -.
DR KEGG; cel:CELE_ZK287.8; -.
DR UCSC; ZK287.8a; c. elegans. [P34704-1]
DR CTD; 179360; -.
DR WormBase; ZK287.8a; CE06617; WBGene00001842; her-1. [P34704-1]
DR eggNOG; ENOG502SXJG; Eukaryota.
DR HOGENOM; CLU_1533954_0_0_1; -.
DR InParanoid; P34704; -.
DR OMA; CCDVFAD; -.
DR OrthoDB; 1592226at2759; -.
DR EvolutionaryTrace; P34704; -.
DR PRO; PR:P34704; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001842; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; P34704; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IDA:WormBase.
DR GO; GO:0005102; F:signaling receptor binding; IDA:WormBase.
DR GO; GO:0030238; P:male sex determination; IMP:WormBase.
DR DisProt; DP02988; -.
DR Gene3D; 1.10.150.370; -; 1.
DR InterPro; IPR015313; Her-1.
DR InterPro; IPR043108; Her-1_C.
DR InterPro; IPR036341; Her-1_sf.
DR PANTHER; PTHR37979; PTHR37979; 1.
DR Pfam; PF09232; Caenor_Her-1; 1.
DR SUPFAM; SSF110014; SSF110014; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..175
FT /note="Protein her-1"
FT /id="PRO_0000021412"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004283"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1SZH"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1SZH"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1SZH"
SQ SEQUENCE 175 AA; 20172 MW; C330DFE9BB3D869A CRC64;
MRYLPIFVFL GSFGYTETTL TKELIKDAAE KCCTRNRQEC CIEIMKFGTP IRCGYDRDPK
LPGYVYKCLQ NVLFAKEPKK KINLDDSVCC SVFGNDQNDS GRRCENRCKN LMTSPSIDAA
TRLDSIKSCS LLDNVLYKCF EKCRSLRKDG IKIEVLQFEE YCNATFIQKR TFRGV
