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NHL1_CAEEL
ID   NHL1_CAEEL              Reviewed;         974 AA.
AC   Q03601; Q23510;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=RING finger protein nhl-1;
GN   Name=nhl-1 {ECO:0000312|WormBase:F54G8.4a};
GN   ORFNames=F54G8.4 {ECO:0000312|WormBase:F54G8.4a};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
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   INTERACTION WITH UBC-13.
RX   PubMed=15530417; DOI=10.1016/j.bbrc.2004.10.047;
RA   Gudgen M., Chandrasekaran A., Frazier T., Boyd L.;
RT   "Interactions within the ubiquitin pathway of Caenorhabditis elegans.";
RL   Biochem. Biophys. Res. Commun. 325:479-486(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18652816; DOI=10.1016/j.ydbio.2008.06.037;
RA   Hyenne V., Desrosiers M., Labbe J.C.;
RT   "C. elegans Brat homologs regulate PAR protein-dependent polarity and
RT   asymmetric cell division.";
RL   Dev. Biol. 321:368-378(2008).
CC   -!- SUBUNIT: Interacts with ubc-13. {ECO:0000269|PubMed:15530417}.
CC   -!- INTERACTION:
CC       Q03601; G5EFS1: ikb-1; NbExp=5; IntAct=EBI-314158, EBI-314119;
CC       Q03601; G5EC32: sorb-1; NbExp=7; IntAct=EBI-314158, EBI-325337;
CC   -!- DISRUPTION PHENOTYPE: Double knockout with par-2 mutant (it5ts)
CC       partially suppresses the lethality phenotype of the par-2 mutant
CC       (it5ts) at 25 degrees Celsius. {ECO:0000269|PubMed:18652816}.
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DR   EMBL; BX284603; CAA79562.1; -; Genomic_DNA.
DR   EMBL; Z22177; CAA79562.1; JOINED; Genomic_DNA.
DR   PIR; E88549; E88549.
DR   PIR; S28275; S28275.
DR   RefSeq; NP_499028.1; NM_066627.5.
DR   AlphaFoldDB; Q03601; -.
DR   SMR; Q03601; -.
DR   BioGRID; 41494; 20.
DR   DIP; DIP-26359N; -.
DR   IntAct; Q03601; 14.
DR   STRING; 6239.F54G8.4; -.
DR   iPTMnet; Q03601; -.
DR   EPD; Q03601; -.
DR   PaxDb; Q03601; -.
DR   PeptideAtlas; Q03601; -.
DR   PRIDE; Q03601; -.
DR   EnsemblMetazoa; F54G8.4a.1; F54G8.4a.1; WBGene00003597.
DR   GeneID; 176295; -.
DR   UCSC; F54G8.4; c. elegans.
DR   CTD; 176295; -.
DR   WormBase; F54G8.4a; CE05942; WBGene00003597; nhl-1.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000168201; -.
DR   HOGENOM; CLU_002505_1_0_1; -.
DR   InParanoid; Q03601; -.
DR   OMA; SEPGCFT; -.
DR   OrthoDB; 489543at2759; -.
DR   PhylomeDB; Q03601; -.
DR   SignaLink; Q03601; -.
DR   PRO; PR:Q03601; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003597; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q03601; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:WormBase.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR   Gene3D; 2.120.10.30; -; 3.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF01436; NHL; 5.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51125; NHL; 6.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..974
FT                   /note="RING finger protein nhl-1"
FT                   /id="PRO_0000055983"
FT   REPEAT          699..742
FT                   /note="NHL 1"
FT   REPEAT          746..788
FT                   /note="NHL 2"
FT   REPEAT          792..835
FT                   /note="NHL 3"
FT   REPEAT          839..883
FT                   /note="NHL 4"
FT   REPEAT          887..930
FT                   /note="NHL 5"
FT   REPEAT          934..974
FT                   /note="NHL 6"
FT   ZN_FING         43..84
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  109138 MW;  A4D195F9AA8BBF72 CRC64;
     MSSSPQNEAE AREKMRELMS RPPSSRPADF VNPLEKIEQL LTCPICLDRY KQPKLLPCQH
     TFCYPCLESC ADTLHRNLKC PECRAEHNIP YDGVKAFQPN YTLTGFLEIH LQATPESAAE
     IEEYIHRYNL ERCKICDEKA DCEPCAHCDR KACKECRQTH MDMLKRDMSR LLNQVKRLAN
     RITEASDNLS KGVDMMTMNC ETTKAEIKEY FHRYQRDLKK KEDNFLMEVD TFQATETRNM
     SNLRDVLEIE SSNMSEAVSR LDAAIKGECS IEDSELVRMK NTFTEGLEYL RNFQPDADEL
     FNRKLRFSAG DDAAKLPAAI TTSGELCVLV PQFSGRYLPL EQSYLPRPFR LPLESDSYRV
     KSDERASMRD READRTSSRH SHRNPEPDES SIRYRRRQQL EDEAWNRLRN SSAAPSLLTT
     SVTADSSSRT SPWAADRVTR SVEPTKSRPT SLIVPNTETP RTVSPASKPP LPPQSVERVE
     RTEDASPAPL PQLPIRKPPL PRQQSSNDDS LNEKVETIRR AHQQRQDASR AASRAVSSEE
     SEGEDFPVST NRGRIRIVCR AASVNRDDGL MSMIPGTGTI INVPPPQHQL PASAPITNGT
     SEQVAIPVTH FTGEEDESDI VVPAWLQRRR QRFQRSRTNP DIQAQFTSAR VQQLLAERQS
     RLDSSTTTDE EKEKLAVLRQ RGRSASREAG EWRARGRPRA VFGRKGAKDG ELNWPRGICA
     LSGGLVATCD SSNHRVCVFD KDGKFVRQFG GYGAGAGQLD SAAGLASSKL RVIVSDRYNH
     RISVFGLEGD HLFSFGGHGQ GNAKFNNPWG VAVDDLGSIY VADKDNHRVQ VFDKNGQFIA
     KFGSFGHLPG QLNSPLFIAV SRVTHHVYVS DSSNHRISVF DPHGVHLFSF GEEGFHGGQF
     KFPRGIAIDS QENLIIADSG NNRIQVFDAQ GQFVSSFGTW GGGAGQLKGV EDVCVTADGS
     IVVTDRENHR IQIF
 
 
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