NBEA_CAEEL
ID NBEA_CAEEL Reviewed; 2507 AA.
AC Q19317; K8ESP0; Q20061;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative neurobeachin homolog;
DE AltName: Full=Suppressor enhancer of lin-12;
GN Name=sel-2; ORFNames=F10F2.1;
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=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 [2] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11102458; DOI=10.1523/jneurosci.20-23-08551.2000;
RA Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B., Petrasch-Parwez E.,
RA Kilimann M.W.;
RT "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi protein
RT homolog implicated in neuronal membrane traffic.";
RL J. Neurosci. 20:8551-8565(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17215302; DOI=10.1242/dev.02767;
RA de Souza N., Vallier L.G., Fares H., Greenwald I.;
RT "SEL-2, the C. elegans neurobeachin/LRBA homolog, is a negative regulator
RT of lin-12/Notch activity and affects endosomal traffic in polarized
RT epithelial cells.";
RL Development 134:691-702(2007).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them to the membrane. May anchor the kinase to
CC cytoskeletal and/or organelle-associated proteins (By similarity).
CC Regulates endosomal traffic in polarized epithelial cells such as the
CC vulval precursor cells and intestinal cells. Thought to act as a
CC negative regulator of lin-12 activity in vulval precursor cells. May
CC have a role in the internalization process from basolateral surface of
CC polarized epithelial cells. {ECO:0000250, ECO:0000269|PubMed:17215302}.
CC -!- SUBUNIT: Interacts with RII subunit of PKA.
CC {ECO:0000250|UniProtKB:Q9EPN1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17215302}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:17215302}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval precursor cells and rectal
CC epithelia in L2 and L3 larvae. In L4 larvae, expression is seen in
CC intestinal epithelial cells. {ECO:0000269|PubMed:17215302}.
CC -!- DISRUPTION PHENOTYPE: Worms lacking sel-2 exhibit a multivulva
CC phenotype when combined with loss of lin-12.
CC {ECO:0000269|PubMed:17215302}.
CC -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC {ECO:0000305}.
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DR EMBL; Z35598; CCO25913.1; -; Genomic_DNA.
DR EMBL; Z46242; CCO25913.1; JOINED; Genomic_DNA.
DR PIR; T20719; T20719.
DR RefSeq; NP_497939.2; NM_065538.5.
DR AlphaFoldDB; Q19317; -.
DR SMR; Q19317; -.
DR BioGRID; 40842; 4.
DR STRING; 6239.F10F2.1; -.
DR iPTMnet; Q19317; -.
DR EPD; Q19317; -.
DR PaxDb; Q19317; -.
DR PeptideAtlas; Q19317; -.
DR EnsemblMetazoa; F10F2.1a.1; F10F2.1a.1; WBGene00004760.
DR GeneID; 175606; -.
DR KEGG; cel:CELE_F10F2.1; -.
DR CTD; 175606; -.
DR WormBase; F10F2.1a; CE32621; WBGene00004760; sel-2.
DR eggNOG; KOG1787; Eukaryota.
DR GeneTree; ENSGT00940000170888; -.
DR HOGENOM; CLU_000218_2_0_1; -.
DR InParanoid; Q19317; -.
DR OMA; XRKVEIM; -.
DR OrthoDB; 153369at2759; -.
DR PhylomeDB; Q19317; -.
DR PRO; PR:Q19317; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004760; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q19317; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; IMP:WormBase.
DR GO; GO:0016197; P:endosomal transport; IMP:WormBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR010508; NBEA-like_DUF1088.
DR InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR InterPro; IPR023362; PH-BEACH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF06469; DUF1088; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF14844; PH_BEACH; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS51783; PH_BEACH; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..2507
FT /note="Putative neurobeachin homolog"
FT /id="PRO_0000051092"
FT DOMAIN 1690..1798
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 1817..2106
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026,
FT ECO:0000305"
FT REPEAT 2265..2308
FT /note="WD 1"
FT /evidence="ECO:0000305"
FT REPEAT 2326..2365
FT /note="WD 2"
FT /evidence="ECO:0000305"
FT REPEAT 2405..2444
FT /note="WD 3"
FT /evidence="ECO:0000305"
FT REPEAT 2447..2486
FT /note="WD 4"
FT /evidence="ECO:0000305"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2507 AA; 281205 MW; D2084909EFCE1C9E CRC64;
MEISETSHNE SGPPVQENGI VEIPVEEGEE VNDEESNMET VDLGLDDSAA DASSPSVFKN
IDDEAPGDPS DAAKKEEDSE EIVVPSVLAP TPSQEVSPPN AIESLPPLPE GKELELEDDV
TSSLPRLLSK TTLIHSNEEG ADETIQRLVT VLHSNSPNTD RTQVVDNLFN LLVGGHFDQE
SKFVIEDAAN VDHMLTLLSH CDYDLQNEIW SLFLAVMKKS NRNLEACTRV GLISKVLDIL
PEAPPLLADL LVQIIAALVA YSINVKQTKH LLRALKSTKE QWPPNSLKLL HVLKEMPQHD
SADVFFSFPG KDQSGIILPP IKTMPYQQGW TFATWLRMEP LNSVTFEKEQ PVLYSFRTSK
GVGYSCHFTG NCLVVNVEKT KGKEQSRCVR AELGARKWHH IAIAHCYSRW GRSDIKCFID
GQLAETIELS WVVTSATNWD RCSIGVSADG TANSAFCGQM GAMYLFAEAL TLQQANSLFC
LGPVYQSTFK HDSETSLPEG YKKHLFDGHL HSSLVFAYCP KNCHGQLCLY TPPKTAASTY
FVQIPHAVMK EGVEVITTHS IHKSLQSVGG IQILLPLFAQ IDLPSSNDNS IDGEVCQTLL
SLIALLLSSS QSSQQQLFHS KGFLIISSCL QKASPSHLSM KVLEQLIHIA KFLLRCPAGG
PLLKHLFDYI LFNPKLWIRA RPEVQVHLYQ YLATDFLANN NFSQMLRRVP TVIEMCHTLK
HFYWLALPQT VSDYTIEERP ENFATADIVA IRSSILTFIN RIIIASAGPE EEERVRDQEV
HTLLNLLATV REDDNLYDVL ALVTRLLAEH PAIMIPAIDK NKALGIIFNL LAAPNELIRI
PALKILGFFL SRSTLKRKTE SMGNQNLFSL IGERLLSHKK VLSLPTYNVL LEILVEQMTP
TFTYACHQPA QPEWKFENPH LLKVIAHVIS QCEESENIVQ IKKCFLIDII NLCRESKENR
RTILQMSVWQ DWLIGLAYVF HTTESQNEVS ELVWEAFSIL LHHALRNEYG GWRVWVDTLA
IAHSKVSFEK FKRKLAEAKI KAERSESGGE EAKMEPTPIY RAPEFAWSDV HVRLLADLLS
GIERVVDEWK VAECGISDQC NASENQVFVG NVVHVVSQLS DSLIMACGGL LPLLASATAP
NNDMEIVDPC QQQLPISVSA GFLMRFARLV DTFVLASGVS FSELEQEKNM PAGGVLRQSL
RISATVTVRH ILASRIQQPD TPRYETNSTK KNQCIMEFVR EALEKRSPDG LENVERLVQD
SDITRIKGVV YRDMVEENRQ AQFLALSVIY LVSVLMVSRY RDILEPPSSP SPFFDSTTQK
QENSENVNSE TSPENGSNGK LANGGDNLSI KNGIESNGND GEEEENGEEG QGDDGGRIAA
IKVANADMKR GDGNEYDEEE LSKMHQSNGR RPSTMMPVQQ TAERRAYLTT KLQTALETCA
PLLREMMSDF RGYLQKTLLG THGQEIMNDT KVLETLRNRN ASVIELVMLL CSQEWQTSLQ
KHAGLAFIEL VNEGRLMAHA TRDHVLRVAN EADFILNRLR AEDVSKHAQF EAESREQLAA
RHEEYGRCDL LIASGRLRDS INATRLLEKM SAILSDQDDS KSGTQFWKLD VWEDDSRRRK
RFVPNAYGSR HEEANLPEGE KNEEPEISEQ EKIRKVLKGL FSKRQNSSGS HELVDESDID
KWAQEVDPTP SSQSACFSTT AKLIAPGVVV PGTLSVTAND LFFDANESDP NYKKQCAQVL
RYCEALHARW NLQEIRAIFL RRYLLQNTAL ELFLASRTAI MFAFDSEDAV KKVVYQLPRV
GVGVKYGLPQ SRKTSLMTPR QLFKHSDMCA KWQKREISNF DYLMFLNTVA GRTFNDLSQY
PVFPWILTNY TSDTLDLSVA SNFRDLSKPI GALSEARRKF FNDRYTSWDD DQVPAFHYGT
HYSTPAFTLN WLLRVEPFAS MFINLHDGKF DHPDRITHSI KDSWDRCQRD SHDVKELIPE
LFYLPEMFRN SSKFNLGRRA DGTPVDDVVL PPWAESPEHF VLMHRQALES DLVSCQLNQW
IDLIFGYKQR GAEAVRATNV FYHLTYEGTV TPKMAETPGQ VAAIEQQILS FGQTPSQLLT
EAHPPRHSIM SMAPTMFRRH DEDLCMMMKY ISNSPVVYLA ANTFHQLPQP TVVGVAQNLV
FSLNKWDNSY SYGASQRSAL SMDPSNAEGQ VSLPLTADAQ LASAASTTPV ARRHLGDAFD
QRLTVQCSNF VTTTDSKFIF ACGYPDYSFR IVDTDSGRVR QAVYGHGDVV TCIARSETSL
FSDCYVVTGS MDCTVVLWHW NGTTGFIAGE YNQPGEVPSP RSILTGHEAS ISALCVSAEH
GLVVSGCEDG VILIHTTSSD LLRRIRGHGI VTQLSMSREC ILLSLFDSKR MVTYSATAKK
LDEVLVDDKI ECVTVTRDGE FAVTGAVNGR INIWRMFPLT KLYTYQPLNS AVRSVAVVAS
HRFILGGLDS GAIVVFNADF NRWHYEYKHR YIQNTSAAKP VQQSPQK
