ID NBEA_CAEBR Reviewed; 2531 AA.
AC A8XSV3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Putative neurobeachin homolog {ECO:0000250|UniProtKB:Q19317};
DE AltName: Full=Suppressor enhancer of lin-12;
GN Name=sel-2 {ECO:0000312|EMBL:CAP35556.1}; ORFNames=CBG18029;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP35556.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP35556.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Regulates endosomal
CC traffic in polarized epithelial cells such as the vulval precursor
CC cells and intestinal cells. Thought to act as a negative regulator of
CC lin-12 activity in vulval precursor cells. May have a role in the
CC internalization process from basolateral surface of polarized
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q19317,
CC ECO:0000250|UniProtKB:Q9W4E2}.
CC -!- SUBUNIT: Interacts with RII subunit of PKA.
CC {ECO:0000250|UniProtKB:Q9W4E2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19317,
CC ECO:0000250|UniProtKB:Q9W4E2}. Membrane {ECO:0000250|UniProtKB:Q19317,
CC ECO:0000250|UniProtKB:Q9W4E2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q19317, ECO:0000250|UniProtKB:Q9W4E2}. Nucleus
CC {ECO:0000250|UniProtKB:Q19317, ECO:0000250|UniProtKB:Q9W4E2}.
CC -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC {ECO:0000255}.
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DR EMBL; HE600963; CAP35556.1; -; Genomic_DNA.
DR RefSeq; XP_002642088.1; XM_002642042.1.
DR AlphaFoldDB; A8XSV3; -.
DR SMR; A8XSV3; -.
DR STRING; 6238.A8XSV3; -.
DR GeneID; 8584083; -.
DR KEGG; cbr:CBG_18029; -.
DR CTD; 8584083; -.
DR WormBase; CBG18029a; CBP44582; WBGene00037526; Cbr-sel-2.
DR eggNOG; KOG1787; Eukaryota.
DR HOGENOM; CLU_000218_2_0_1; -.
DR InParanoid; A8XSV3; -.
DR OMA; XRKVEIM; -.
DR OrthoDB; 5478899at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.1540.10; BEACH domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR046851; NBCH_WD40.
DR InterPro; IPR010508; NBEA-like_DUF1088.
DR InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR InterPro; IPR046852; Neurobeachin_a-sol.
DR InterPro; IPR023362; PH-BEACH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13743; BEIGE/BEACH-RELATED; 1.
DR PANTHER; PTHR13743:SF160; NEUROBEACHIN; 1.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF06469; DUF1088; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF20426; NBCH_WD40; 1.
DR Pfam; PF20425; Neurobeachin; 1.
DR Pfam; PF14844; PH_BEACH; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF81837; BEACH domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS51783; PH_BEACH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Membrane; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..2531
FT /note="Putative neurobeachin homolog"
FT /id="PRO_0000372678"
FT DOMAIN 1714..1822
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 1841..2130
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 2289..2332
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 2350..2389
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 2429..2468
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 2471..2510
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2531 AA; 284664 MW; 938F1958E0CA0281 CRC64;
MDISETEYND SDPPVQENGN GKAVVEDEVN DEESNMETVD LGLDDKTSDA SSQNVFKNID
NEPSDDQQNV EESENITLEK PEEISAPPTV VSTSQDVSPP PAIESLPPLL EGKELELEDD
VTSSLPRLLS KTTLIHSNEE GADETIQRLI SSLHSNSPNM DRTQIVDHLF NLLVGGHFDQ
ESKFVIEHVA NVDHMLTLLS HCDCDLQNEI WSLFLAVMKK SNRNLEACTR VGLISKNFFL
NLVLDLLPEA PPLLADLLVQ IIAALVAYSI NVKQTKHLLR ALRSTKDQWP PNSLKLLHVL
KEMPQHDSAD VFFSFPGKDQ SGIILPPIKT MPYQQGWTFA TWLRMEPLNS VTFEKEQPVL
YSFRTSKGIG YSCHIFGNCL VVNVEKAKGK EQSRCVKAEL GARKWHHIAI AHCYSRWGRS
DIKCFIDGQL AETIELSWVV TSTTSWDRCS IGVSADGAVN TAFCGQMGAM YLFAESLSLQ
QANSLFCLGP AYQSTFKHDS ETSLPEGYKK HLFDGHLHSS LVFAYCPKNC HGQLCLFTPP
KTAANTYFVQ IPHAVMKEGV EVITTHSIHK SLQSVGGIQI LLPLFAQIDL PSSHDNTIDG
DVCQTLLSLI SLLLSSSQSS QQQLFHSKGF LIISSCLQEA SPSHLSMKVL EQIIHIAKFL
LRCPAGGPLL KHLFDYILFN PKLWIRARPE VQVHLYQYLA TDFLANNNFS QMLRRVPTVI
EMCHTLKHFY WLALPQTVSD YTVEERPENF ATAEIVSIRS AILTFINRII ISSNSPDEEE
KARDQEIHTL LNLLATVRED DNLYDVLALV TRLLAEHPAI MIPAIDKNKA LGIIFNLLAA
PNELIRIPAL KILGFFLSRS TLKRKTESMG SQNLFSLIGE RLLSHKRTIS LPTYNVLLEV
LVEQMTPTFT YAAHQPAQPD WKFENPHLLK VIAHVISQCE ETESLVQIKK CFLIDIINLC
RESKENRRTI LQMSVWQDWL IGLAYVFHTS ESQNEVSELV WEAFSILLHH ALRHEYGGWR
VWVDTLAIAH SKVSYEKFKR RLAEAKAKAE KAETGEEAKM EPTPVYRAPE FAWSEVHIRL
LADLLSGIER TVEEWKTQEG GISDQCNASE NQVFVGNVVH VISQLADSLI MACGGLLPLL
ASATAPNNDM EIVDPCQQQL PISVAASFLM RFAKLVDTFV LASGVSFSEL EQEKNMPAGG
VLRQSLRISA TVTVRHILAS RIQQPDTPRY ETNSAKKNQC IMDFVKEALE NFSPEGLENV
ERLVQDSDIT RIKGVVYRDM VEENRQAQFL ALSVIYLVSV LMVSRYRDIL EPPSSPSPFF
DSTTTKQENA ERGEKLFEFS HNPLFLELPE SSSEAVANGK VANDGDHASI KNGSDHSENG
ADEETEEKGE QGQGDNGGTI AAIKVANSDM KNDGNEYNEE ELKKMHQSNG RRPSTLMPPQ
QTAERRAYLT TKLQTALETC APLLREMMSD FRGYLQKTLV GTHGQEIMND TKVLETLRNR
NASVIELVML LCSQEWQTSL QKHAGLAFIE LVNEGRLMAH ATRDHVLRVA NEADFILNRL
RAEDVSKHAQ FEAESREQLN ARYEEYSRCD LLIVSGRLRD SLNATRLLDK MSAILTDGDD
SKSGSQFWKL DVWEDDSRRR KRFVPNPYGS RHEEANLPEG EKNEEPEISE QERIRKILKG
LFSQRHATTT STGGQELVDE SDIDKWAQEV DPTPSSQSAC FSTAAKLIVP GVVVPGTLSV
TASDLFFDAN ESDPNYKKQC AQVLRYCEAL HARWNLQEIR AIFLRRYLLQ NTALEMFLAS
RTAIMFAFDS EDTVRKVVYQ LPRVGVGVKY GLPQSRKTSL MTPRQLFKHS DMCAKWQKRE
ISNFDYLMFL NTVAGRTFND LSQYPVFPWI LTNYTSDTLD LSVASNFRDL SKPIGALNEA
RRKFFTDRYA SWDDDLVPAF HYGTHYSTPA FTLNWLLRLE PFASMFINLH DGKFDHPDRI
THSIKDSWDR CQRDSHDVKE LIPELFYLPE MFRNSSKFNL GRRADGTLVD DVVLPPWAES
PEHFVLMHRQ ALESDLVSCQ LNQWIDLIFG YKQRGAEAVR ATNVFYHLTY EGTVTQKMAE
TPGQVSAIEQ QILSFGQTPS QLLAEAHPPR HSIMTMAPTM FRRHDDDLCM MMKYISNSPV
VYLAANTFHQ LPHPTVVGVA QNLVFSLNKW DNSYSYGSTQ RSALSMDPSN VEGQVALPLT
ADPQLATAAS TTPIARRHLG DAFDQRLQVQ CSNFVTTTDS KYIFACGYPD YSFRIVDTDS
GRVRQAVYGH GDVVTCIARS ETSLFSDCYV VTGSMDCTVV LWHWNGTTGF IAGEYNQPGE
VPSPRSILTG HEASISALCV SAEHGLVVSG CEDGVILIHT TASDLLRRIR GHGTVTQLSM
SRECILLVLF DSKRMTTYSS TARKLNEVLS EEKIECVTVT RDGEFAVTGA VNGRITIWRM
FPLNKLYTYQ PLNSAVRSVA VVASHRFILG GLDSGAIVVF NADFNRWHYE YKHRYIQNSS
ATKPAQASPQ K
//
