ID A0A7E6E4R6_9CHIR Unreviewed; 2715 AA.
AC A0A7E6E4R6;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 08-OCT-2025, entry version 22.
DE RecName: Full=Neurobeachin-like protein 2 {ECO:0000256|ARBA:ARBA00068540};
GN Name=NBEAL2 {ECO:0000313|RefSeq:XP_035886314.1};
OS Phyllostomus discolor (pale spear-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae;
OC Phyllostominae; Phyllostomus.
OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_035886314.1};
RN [1] {ECO:0000313|RefSeq:XP_035886314.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_035886314.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
CC -!- FUNCTION: Probably involved in thrombopoiesis. Plays a role in the
CC development or secretion of alpha-granules, that contain several growth
CC factors important for platelet biogenesis.
CC {ECO:0000256|ARBA:ARBA00056842}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC {ECO:0000256|ARBA:ARBA00008498}.
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DR RefSeq; XP_035886314.1; XM_036030421.1.
DR GeneID; 114501539; -.
DR CTD; 23218; -.
DR Proteomes; UP000504628; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0019901; F:protein kinase binding; IEA:TreeGrafter.
DR GO; GO:0030099; P:myeloid cell differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0008104; P:protein localization; IEA:TreeGrafter.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR FunFam; 1.10.1540.10:FF:000001; neurobeachin isoform X1; 1.
DR FunFam; 2.130.10.10:FF:001375; Neurobeachin-like protein 2; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.10.1540.10; BEACH domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR050865; BEACH_Domain.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR046851; NBCH_WD40.
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:SF111; NEUROBEACHIN-LIKE PROTEIN 2; 1.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF16057; DUF4800; 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; 3.
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.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000504628};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 1883..2008
FT /note="BEACH-type PH"
FT /evidence="ECO:0000259|PROSITE:PS51783"
FT DOMAIN 2021..2313
FT /note="BEACH"
FT /evidence="ECO:0000259|PROSITE:PS50197"
FT REPEAT 2459..2492
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2510..2551
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1274..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1351
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2715 AA; 298239 MW; EB45D9410DFF0967 CRC64;
MAASERLYEL WLLYYTQKDL GYLQQWLKAF VGTFEKSISI SSLEPRRPEE AGAEVPLLPL
DPLQVLAEQL DEGDLEQTLL LLKLFIVLCR NLDNVEAGWG RVLVPRVLAL LSRLVAKLKG
SPPLQEGQGP KLEEVALHAL LLSEGLFDPY QTWRRQHSGE VISAKEKSKY KFPPAALPAE
FRGFFPESLQ DADRLPPTLL LRLIHLFGAI LAGGTENGQV AVSAGSVQGL LDVVQGCGRG
PAPDSRQVSL ALEALVGAAH VLHTSRTPHR APELRMLLEG YFRVLNADWP AGPNPGPEEA
LVSLRVSMLD AIPMMLACED RPVLQATFLS NNCFEHLIRL IQNSKVLDQD TDAIAVHVVR
VLTCIMSGSP SAKEVFKERI GYPHLHEVLQ SHGPPTHRLL QELLNMAVEG DHSTCPPPPI
RNEQPVLVLM RWLPALPTAE LRLFLAQRLR WLCDSCPASR ATCVQAGLVG CLLETLGVGE
ALGARCQEQL LALLQALGRV SLRPLELRRL LRPPPGLDSG PGGAEAGQAR HAGAIIRALS
GMARHQGPAR ALHYFDLTPS MAGIMVPPVQ RWPGTGFTFH AWLCLHPTAA APAQAPTRPL
QRKQLYSFFT SSGSGFEAFF TAAGALVVAV CTRKEYFTLS LPDVTFADSA WHCVTVVHAP
GRRIFSQNLA HVYKDGVLVK TASLRCPSLS EPFSSCCIGS AGHRTTTTTT GPPAPPVPTA
MAHAHPSLTR SQSVPATTEL GRGSGLTAPL QEGSISSTLA GTQDTRWGSP TSLEGQLGAV
AIFHEALQAE DLRVLCTLGP NETAPFKPES ELHELDTKLL LHYSPQACKN NICLDLSPGH
GLDGRLTGHT VEAWDVKDVV SCVGGMGALL PLLEHVAAQP QAAEAGPAET HDLVGPELTS
GHNSQGLLLP LGKSSEERME RNAVAAFLLM LRNLLQGHAV NQDSLVKCKG PAIVGALLRK
VPSWAMDMNV LMSAQLLMEQ VAAEGGGPLL YLLYQHLLFN FHLWALSDFA VRLGHIQYMS
SIVREHRQKL RKKYGVQFIL DALRTHYSPQ RERPLAADDL RTVQTSLLGL AREFLVRSPS
ADDLQVVLNF LAASGDDGQV LGVLDLLLAL LQSSSTQDFL AAFLLGPGSL EVLLALLVQP
RSLPLLSDRV CQILRRLRQN ERLSEQSHQR LWLRECGLQG LVACLPEAAV SLQLCQNLYK
LFLGTDCPNL SDLMAVVQLS LQADLSVRLY ICRQLFHLIH KQPDVVRLLA RQAGWQDVLT
RLYVLEAATA GSPLPFPPEQ PASPEPAVPK PHSESPDPSD VFLPSEAPCP DPDALYQALS
PFCASFDLGL ERSSMGSGST TGGGGGGGGS GTLTPASQPG TPSPLDGPRP FPAARGRHSS
SLSNVLEDGS LPEPTVSGDD ISNTSNPQQT PEEELCNLLT NVLFLVMWRG VEGSDEASWR
ERGQVFSVLT QLGASATLVR PPDCIKRSLL EMMLESALTD IKEAPPGALA SLIQQVLWLL
RLLQDFLCAE GHGNQELWSE KLFEGVCSLL DRLGAWPHLA GSPSDLREMA QIGLHLVLGY
ILLEDPQLHA QAHVRLHSLL QTAVPMRREE ACYVLSKLEA VLSRALHACD VAAEDQEPPA
RAAAFTERCS WLVPLVRTLL DRAYEPLGLQ WGLPSLPPTN GSPTFFEDFQ DFCATPEWRH
FIDKQVQPTM SQFEMDTYAK SHDLMSGFWN SCYDTLMSSG QRRQQERAHS HRDFQKLVLE
PVQRRARQEG LRYASVLKQQ AAQHSSVLLH WGALWRQLSC PCGAWALRDP PTPRWKMSSA
ETYSRMRLKL VPNHRFNSHL EASALRDNLG EAPLTATEEA SLPLAVTKEA KVSTLPEELQ
EDQLGEDELA SLETTMQAAE LDEQHEKLVL SAECQLVTIV AVVPGLLEVT TQHIYFYDGS
AEHVETEEGI GHNFQRPLAQ LREVHLRRFN LRRSALELFF IDQANYFLNF PCKAGGAAAS
SPCQSPRPQP HPIPPHTQIR NQVYKWLLRL RPPAQGYLSS RSPQEMLRAS GLTQKWVQRE
ISNFEYLMQL NTIAGRTYND LSQYPVFPWV LQDYVSPTLD LSNPAVFRDL SKPIGVVNPK
HAQLVREKYE SFEDPAGTID KFHYGTHYSN AAGVMHYLIR VEPFTSLHVQ LQSGRFDCSD
RQFHSVAAAW QARLDSLADV KELIPEFFYF PDFLENQNGF DLGCLQLTNE KVGDVVLPPW
ASSPEDFIQQ HRQALESEYV SAHLHKWIDL IFGYKQRGPA AEEALNVFYY CTYEGAVDLD
HVADERERKA LEGIISNFGQ TPCQLLKEPH PARLSAEEAA QRLARLDTNS PSIFQHLDQL
KAFFAEVISD GVPLVLAVVP HRQLHSFMAP DLLVTVSASG LLGTHSWLPY DRNISNYFSF
IKDSNKVQRF LSGPWVQDSG VSGQALAVTP DGKLLFSGGH WDGSLRVTAL NRGKLLNQIS
RHLDIVTCLA LDTCGIYLIS GSRDTTCMVW RLLQKDGVSG GLASKPMQVL YGHEAAVSCV
AISTELDMAV SGSEDGTVII HTVRRGQFVA ALRPPGATLP GPVSHLALGS EGQIVVQSSA
RERLGAQATY SLHLYSVNGR LRASLPLVEQ PTALAVTEDF VLLGTAQCAL HILHLNKLLP
AAPPLPMKVP IRSLAVTKER SHVLVGLEDG KLIVVGAGQP SEVRSIQFTR KLWRSSRRIS
QVSSGETEYK PEEAR
//
