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   03-AUG-2022, entry version 81.
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.CBG18029; -.
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; 153369at2759; -.
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; 1.10.1540.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 2.
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.
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