ID U3KMJ1_RABIT Unreviewed; 1381 AA.
AC U3KMJ1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Pleckstrin homology like domain family B member 2 {ECO:0000313|Ensembl:ENSOCUP00000026449.2};
GN Name=PHLDB2 {ECO:0000313|Ensembl:ENSOCUP00000026449.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000026449.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000026449.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000026449.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000026449.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000026449.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAGW02015727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02015728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; U3KMJ1; -.
DR STRING; 9986.ENSOCUP00000026449; -.
DR PaxDb; 9986-ENSOCUP00000026449; -.
DR Ensembl; ENSOCUT00000033401.2; ENSOCUP00000026449.2; ENSOCUG00000003962.4.
DR eggNOG; ENOG502QUWG; Eukaryota.
DR GeneTree; ENSGT00940000156371; -.
DR InParanoid; U3KMJ1; -.
DR Proteomes; UP000001811; Chromosome 14.
DR Bgee; ENSOCUG00000003962; Expressed in heart and 17 other cell types or tissues.
DR ExpressionAtlas; U3KMJ1; baseline.
DR GO; GO:0045180; C:basal cortex; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IEA:Ensembl.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IEA:Ensembl.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR CDD; cd14673; PH_PHLDB1_2; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037810; PHLDB1/2/3_PH.
DR PANTHER; PTHR12156:SF21; PLECKSTRIN HOMOLOGY-LIKE DOMAIN FAMILY B MEMBER 2; 1.
DR PANTHER; PTHR12156; PLECKSTRIN HOMOLOGY-LIKE DOMAIN, FAMILY B, MEMBER 3; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 1271..1374
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..731
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 761..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1163..1222
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 155412 MW; F279021E2F8BAFBB CRC64;
MDSSVSSEMQ QARLMEGDDT QREEPEGDGA CDAQHSDFSN MMAEHSHVQN RQDLQNGSVE
EGFVVHSLEN DPQNVMENLG PKKYSSSLRF KANGDYSGSY LTLSQPVPTK RSPSPLGTGV
RSSPSLAKIQ GSKQLSCDGT DKSMSMKPPT PLLSTTPSGY LLGRADFENY TGRDSEKSLR
LSEKPPYCKY SSRNKSHDNV YFLGGLEGRK ASGSLLAMWS AGALGDTGPS PISRSGAASM
PSSPKQARRM NMQDNLTLQP RSSRHRELAS ENTSGRTRKY SGSSLSHMGA YSRSLPRLYK
ATENQLTPLS LPPRHSLGNS KRTKLGEKDL PHSLVDNDNY LNFSSLSSGA LPYKTSASEG
NPYVSSTLSV PASPRVARKM LLASTSSCAS DDLDRAPYPG SSPNHSFPPG EPDRLFVARR
NFSCGSVELD DADLDSLRQA SGTPQPALRE RKSSISSISG RDDLMDYHRR QREERLREQE
MERLERQRLE TILSLCAEYT KPDSRLSSGT TVADVQKINK ELDKLQLSDE ESVFEEALAS
ADSRYRCHRK GSLHDADLAG FGSLGQSGGS FLAPRSIRNE ELLRDLTRTP PPPPSAFLKA
SSESSYLSIL PKTPEGVSEE QRAQELAAME DARIVILNNL EELEQKIKDI NDQMDESSRE
LDMECALLDG EQKSETTELM KEKEILDHLN RKIAELEKNI VGEKTKEKVK LDAEREKLER
LQELYSEQKT QLDNCPESMR EQLQQQLKRD ADLLDVESKH FEDLEFQQLE HESRLDEEKE
NLTQQLLREV AEYQRNIVTR KEKISALKKQ ANHIVQQAQR EQDHFVKEKN NLIMMLQREK
ENLCNLEKKY SSLSGGKGFP VNPSTLKEGY ITVNEINEPC GNSTTLSPST QFPADADADA
VATEPATAVL ASQPRSKEQS SPVCSGFVFP STLSAHPVTQ PPSDSWPEVM APSIEPFPLN
DTPPPLPAKK HRRQQPQEQQ HFRSLEERKK QHKEGLYLSD TLPRKKTTPS ISPHFSSATM
GRCTTPKAHL PLGQSNSCGS VLPHSLATMT KDSESRRMLR GKSKKGRMNS SAGAITNSKS
SSIKGYNHQQ MSEGQRQKSS EFYNRTASES NVYLNSFHYP DHSYKDQAFD TLSLDSSDSM
ETSISACSPD NISSASTSNI ARIEEMERLL KQAHAEKTRL LESREREMEA KKRALEEEKR
RRELLEKRLQ EETSQRQKLI EKEVKIREKQ RAQARPLTRY LPVRKEDFDL RSHVETAGHN
IDTCYHVSIT EKTCRGFLIK MGGKIKTWKK RWFVFDRNKR TFSYYADKHE AKLKGVIYFQ
AIEEVYYDHL KNANKSPNPL LTFSVKTHDR IYYMVAPSPE AMRIWMDVIV TGAEGYTHFL
L
//
