ID A0A287AXI4_PIG Unreviewed; 4772 AA.
AC A0A287AXI4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RCR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012249};
DE EC=2.3.2.33 {ECO:0000256|ARBA:ARBA00012249};
GN Name=MYCBP2 {ECO:0000313|Ensembl:ENSSSCP00000048862.2,
GN ECO:0000313|VGNC:VGNC:90502};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000048862.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000048862.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000048862.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000048862.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC EC=2.3.2.33; Evidence={ECO:0000256|ARBA:ARBA00000333};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
CC -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family.
CC {ECO:0000256|ARBA:ARBA00005415}.
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DR Ensembl; ENSSSCT00000043213.3; ENSSSCP00000048862.2; ENSSSCG00000009473.5.
DR VGNC; VGNC:90502; MYCBP2.
DR GeneTree; ENSGT00940000155756; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome 11.
DR Bgee; ENSSSCG00000009473; Expressed in penis and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287AXI4; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:1902667; P:regulation of axon guidance; IEA:Ensembl.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR CDD; cd19799; Bbox2_MYCBP2; 1.
DR CDD; cd16463; RING-H2_PHR; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.120.820; PHR domain; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45943; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR PANTHER; PTHR45943:SF1; E3 UBIQUITIN-PROTEIN LIGASE MYCBP2; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287AXI4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 601..656
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 959..1009
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 1010..1067
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2341..2434
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 3812..3990
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 4522..4573
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 87..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2807..3025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3073..3114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3160..3180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3699..3723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4009..4030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2807..2829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2830..2851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2877..2944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2954..2984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4013..4027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4772 AA; 523934 MW; CC5448F1770549FB CRC64;
MMMCAATASP AAASSGPGGD GFFPAATISS SPAPGALFMP VPEGSLAAAG LGLGLPAADS
RGHYQLLLSG RALADRYRRI YTAALSDRDQ GGSSAGHPAS RNKKILNKKK LKRKQKSKSK
VKTRSKSENL ENTVIIPDIK LHSNPSAFNI YCNVRHCVLE WQKKETSLAA ASKNSVQSGE
SDSDEEEESK EPPIKLPKII EVGLCEVFEL IKETRFSHPS LCLRSLHALL NVLQGQQPEG
LQSEPPEVLE SLFQLLLEIT VRSTGMNDST GQSLTALSCA CLFSLVASWG ETGRTLQAIS
AILTNNGSHA CQTIQVPMIL NSLQRSVQAV LVGKIQIQDW FSNGIKKAAL MHKWPLKEIS
VDEDDQCLLQ NDGFFLYLLC KDGLYKIGSG YSGTVRGHIY NSTSRIRNRK EKKSWLGYAQ
GYLLYRDVNN HSMTAIRISP ETLEQDGTVM LPDCHTEGQN ILFTDGEYIN QIAASRDDGF
VVRIFATSTE PVLQQELQLK LARKCLHACG ISLFDLEKDL HIISTGFDEE SAVLGAGREF
ALMKTANGKI YYTGKYQSLG IKQGGPSAGK WVELPITKSP KIVHFSVGHD GSHALLVAED
GSIFFTGSAS KGEDGESTKS RRQSKPYKPK KIIKMEGKIV VYTACNNGSS SVISKDGELY
MFGKDAIYSD SSSLVTDLKG HFVTQVAMGK AHTCVLMKNG EVWTFGVNNK GQCGRDTGAM
NQGGKGFGVE NMATAMDEDL EEELDEKDEK SMMCPPGMHK WKLEQCMVCT VCGDCTGYGA
SCVSSGRPDR VPGGICGCGS GESGCAVCGC CKACARELDG QEARQRGILD AVKEMIPLDL
LLAVPVPGVN IEEHLQLRQE EKRQRVIRRH RLDEGRGPLV FAGPIFMNHR EQALARLRSH
PAQLKHKRDK HKDGSGERGE KDASKITTYP PGSVRFDCEL RAVQVSCGFH HSVVLMENGD
VYTFGYGQHG QLGHGDVNSR GCPTLVQALP GPSTQVTAGS NHTAVLLMDG QVFTFGSFSK
GQLGRPILDV PYWNAKPAPM PNIGSKYGRK ATWIGASGDQ TFLRIDEALI NSHVLATSEI
FASKHIIGLV PASISEPPPF KCLLINKVDG SCKTFNDSEQ EDLQGFGVCL DPVYDVIWRF
RSHTRELWCY NAVVADARLP SAADTQSRCS ILSPELALPA GPRALTTRSH AALHILGCLD
TLATMQDLKM GIASTEEETQ AVMKVYSKED YSVVNRFESH GGGWGYSAHS VEAIRFSADT
DILLGGLGLF GGRGEYTAKI KLFELGPDGG DHETDGDLLA ETDVLAYDCA AREKYAMMFD
EPVLLQAGWW YVAWARVSGP SSDCGSHGQA SITTDDGVVF QFKSSKKSNN GTDVNAGQIP
QLLYRLPTSD GSASKGKQQT SEPVHILKRS FARTVSVECF ESLLSILHWS WTTLVLGVEE
LRGLKGFQFT ATLLDLERLR FVGTCCLRLL RVYTCEIYPV SATGKAVVEE TSKLAECIGK
TRTLLRKILS EGVDHCMVKL DNDPQGYLSQ PLSLLEAVLQ ECHNTFTACF HSFYPTPALQ
WACLCDLLNC LDQDIQEANF KTSSSRLLAA VMSALCHTSV KLTSIFPIAY DGEVLLRSIV
KQVSTENDST LVHRFPLLVA HMEKLSQNEE NISGMTSFRE VLEKMLVIVV LPVRNSLRRE
NELFSSHLVS NTCGLLASIV SELTASALGS EVDGLNSLHS VKASANRFTK TSQGRSWNTG
NGSPDAICFS VDKPGIVVVG FSVYGGGGIH EYELEVLVDD SEHAGDSTHS HRWTSLELVK
GTYTTDDSPS DIAEIRLDKV VPLKENVKYA VRLRNYGSRT ANGDGGMTTV QCPDGVTFTF
STCSLSSNGT NQTRGQIPQI LYYRSEFDGD LQSQLLSKAN EEDKNCSRAL SVVSTVVRAA
KDLLHRALAV DADDIPELLS SSSLFSMLLP LIIAYIGPVA AAVPKVAVEV FGLVQQLLPS
VAILNQKYAP PAFNPNQSTD STTGNQPEQG LSACTTSNHY AVIESEHPYK PACVMHYKVT
FPECVRWMTI EFDPQCGTAQ SEDVLRLLIP VRTVQNSGYG PKLTSVHENL NSWIELKKFS
GSSGWPTMVL VLPGNEALFS LETASDYVKD DKASFYGFKC FAIGYEFSPG PDEGVIQLEK
ELANLGGVCA AALMKKDLAL PIGNELEEDL EILEEAALQV CKTHSGILGK GLALSHSPTI
LEALEGNLPL QIQSNEQSFL DDFIACVPGS SGGRLARWLQ PDSYADPQKT SLILNKDDIR
CGWPTTITVQ TKDQYGDVVH VPNMKVEVKA VPVSQKKTSL QQEQVKKPQR IPGSPAVTAA
SSNADMTFGG LESPKLDVSY EPMIVKEARY IAITMMKVYE NYSFEELRFA SPTPKRPSEN
MLIRVNNDGT YCANWTPGAI GLYTIHVTID GIEIDAGLEV KVKDPPKGMI PPGTQLVKPK
TEPQPNKVRK FVAKDSAGLR IRSHPSLQSE QIGIVKVNGT VTFIDEIHND DGVWLRLNDE
TIKKYVPNMN GYTEAWCLSF NQHLGKSLLV PVDEPKTNTD DFFKDINSCC PQEATMQEQD
MPFLRGGPGM YKVVKTGPSG HNIRSCPNLR GIPIGMLVLG NKVKAVGEVT NSEGTWVQLD
KNSMVEFCES DEGEAWSLAR DRGGNQYLRH EDEQVLLDQN SQTPPPSPFS VQAFNKGASC
SAQGFDYGLG NNKVLTVLPT TGDQLSAILN SIQSRPNLPA PSIFDQAAKP PSSLVHSPFV
FGQPLSFQQP QLQKSPSRNL ASRERFYKNY GVAGPASALS SLSHKLKGDR GTISTSSRPL
CTPGKSELSS KHSRTLKPDG RMSRTTVEQK KPRGTEGLSA SESLMLKSDA AKLRSDSHSR
SLSPNHNTLQ TLKSDGRMSS SFRAESPGPG SRSSSPKPKT LPASRSSPSG ASSPRSSSPH
DKNLPQKSAA PVKTKLDPPR ERSKSDSYTL DPDTLRKKKM PLTEPLRGRS TSPKPKPVPK
DSKESPGSEN RAPSPHVVQE NLHSEVVEVC TSSTLKTNSV TDSTCDESSE FKSVDEGSNK
VHFSIGKAPL KDEQEMRASP KISRKCANRH TRPKKEKSSF LFKGDGSKPL EPAKQAMSPS
VAECARAVFA SFLWHEGIVH DAMACSSFLK FNPELSKEHA PIRSSLNSQQ PTEEKETKLK
NRHSLEISSA LNMFNIAPHG PDISKMGSIN KNKVLSMLKE PPLHEKCEDG KTEATFEMSV
HHPMKSKSPL PLTLQHLVAF WEDISLATIK AASQNMIFPS PGSCAVLKKK ECEKENKKAK
KEKKKKEKTE VRPRGNLFGE MAQLAVGGPE KDTICELCGE SHPYPVTYHM RQAHPGCGRY
AGGQGYNSIG HFCGGWAGNC GDGGIGGSTW YLVCDRCREK YLREKQAAAR EKVKQSRRKP
MQVKMPRALP TMEAHQVIKA NALFLLSLSS AAEPSILCYH PAKPFQSHLP SVKEGISEDL
PVKMPCLYLQ TLARHHHENF VGYQDDNLFQ DEMRYLRSTS VPAPYISVTP DASPNVFEEP
ESNMKSMPPS LETSPITDTD LAKRTVFQRS YSVVASEYDK QHSILPARVK AIPRRRVNSG
DTEVGSSLLR HPSPELSRLI SAHSSLSKGE RNFQWPVLAF VIQHHDLEGL EIAMKQALRK
SACRVFAMEA FNWLLCNVIQ TTSLHDILWH FVASLTPAPV EPEEEEDEEN KTNKENAEQE
KDTRVCEHPL SDIVIAGEAA HPLPHTFHRL LQTISDLMMS LPSGSSLQQM ALRCWSLKFK
QSDHQFLHQS NVFHHINNIL SKSDDGDSEE SFSISIQSGF EAMSQELCIV MCLKDLTSIV
DIKTSSRPAM IGSLTDGSTE TFWESGDEDK NKTKNITINC VKGINARYVS VHVDNSRDLG
NKVTSMTFLT GKAVEDLCRI KQVDLDSRHI GWVTSELPGG DNHIIKIELK GPENTLRVRQ
VKVLGWKDGE STKIAGQISA SVAQQRNCEA ETLRVFRLIT SQVFGKLISG DAEPTPEQEE
KALLSSPEGE EKVYNATSDA DLKEHMVGII FSRSKLTNLQ KQVCAHIVQA IRMEATRVRE
EWEHAISSKE NANSQPNDED ASSDAYCFEL LSMVLALSGS NVGRQYLAQQ LTLLQDLFSL
LHTASPRVQR QVTSLLRRVL PEVTPNRLAS IIGVKSLPPA DISDIIHSTE KGDWNKLGIL
DMFLGCIAKA LTVQLKAKGT TITGTAGTSV GKGVTTVTLP MIFNSSYIRR GESHWWMKGS
TPTQISEIII KLIKDMAAGH LSEAWSRVTK NAIAETIIAL TKMEEEFRSP VRCIATTRLW
LALASLCVLD QDHVDRLSSG RWMGKDGQQK QMPMCDNHDD GETAAIILCN VCGNLCTDCD
RFLHLHRRTK THQRQVFKEE EEAIKVDLHE GCGRTKLFWL MALADSKTMK AMVEFREHTG
KPTTSSSEAC RFCGSRSGTE LSAVGSVCSD ADCQEYAKIA CSKTHPCGHP CGGVKNEEHC
LPCLHGCDKN ASTLKQDADD MCMICFTEAL SAAPAIQLDC SHVFHLQCCR RVLENRWLGP
RITFGFISCP ICKNKINHTV LKDLLDPIKE LYEDVRRKAL MRLEYEGLHK SEAITTPGVR
FYNDPAGYAM NRYAYYVCYK CRKAYFGGEA RCDAEAGQGD DYDPRELICG ACSDVSRAQM
CPKHGTDFLE YKCRYCCSVA VFFCFGTTHF CNACHDDFQR MTSIPKEELP HCPAGPKGKQ
LEGTECPLHV VHPATGEEFA LGCGVCRNAH TF
//
