ID A0A2U9CYS5_SCOMX Unreviewed; 1621 AA.
AC A0A2U9CYS5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative zinc finger homeobox protein 2 isoform 2 {ECO:0000313|EMBL:AWP20856.1};
GN ORFNames=SMAX5B_002046 {ECO:0000313|EMBL:AWP20856.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP20856.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP20856.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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DR EMBL; CP026263; AWP20856.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000032886; -.
DR OMA; DNENEMG; -.
DR Proteomes; UP000246464; Chromosome 21.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00086; homeodomain; 3.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 3.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45891; ZINC FINGER HOMEOBOX PROTEIN; 1.
DR PANTHER; PTHR45891:SF3; ZINC FINGER PROTEIN 2; 1.
DR Pfam; PF00046; Homeodomain; 2.
DR Pfam; PF12874; zf-met; 2.
DR SMART; SM00389; HOX; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 171..200
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 226..255
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1084..1144
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1413..1473
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 1086..1145
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 1415..1474
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 63..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 174964 MW; D4768B3CE6408CF3 CRC64;
MQEESGETLS SESNGVSEWL CPLCQQGQTD RSSLSLHLTE QHSVLPSCVD RLLDIAVLKL
GASGGEEDKG AQKSSDSESS QPKHAEDDVT SEPGQSSKSS DATPTLVDKE MEEERIIEQG
GVFPSSEPEE EGNELTGAKR QNATENTEIP DASEQSVGKN GVPAENNTRS FKCNACLETF
ASRTALSVHY NSASHIQRMT TGFAESDPQF PSVPVLPRPF VSNKPYQCAV CRVSYNHAIT
LESHMKSVLH QTRSRNAGIV AHAATSTVAT AGLGGITPTA PNAVVSTPGS VSTQLVTTTN
CAAPGTVMVT TTKDGEQIQT SQVAPSLLTS PVASAQAVSA FLTLLTSSPN TLSHSLLPSL
FAAGAAPGAA THQLVPHPQM VMPLILNGLQ AQTQQHQENQ QGQLLTQCVP FVGLSTAQQA
LLTQRLSSLQ SQWPSAGLTT NVSQPCPEEQ KQTINCEREQ ERQDSDETVE EEVSAQIKDS
DNKMTVNNKT EKLKKEDTKE AQCPNIEKKV KAENSEDNGE THRDSTTDGG RSTNQLDLEG
DKAASLNLSP AGTEKSLRNN SLSPSASVPS NSTLSPVHLN LTLSPDSTPQ KSQSGTSPCG
CLGTPKSSPN TNALTNNQTR SHCSTIGSIY SELPVLSEFQ SEVLWAFFES RSAADAASPP
REDCEALGRE VGLSEDEVRR WLSQARQAKR RQRATESDRL QSSAGFTRHS QSSDYDDEES
SLIIAEGEDD AEASGSQAID LSSTRGKRRP RDLGVEGQGD SCLTSDSENE VYTSVIVSDE
ESQSGSVREG TESPAKGEAL REVHADKGSV GGKVLRSTTV FLSDAEDEYE DEEGGGGQRS
KRKKRKGEFE RDEVEVKKER QDPDVDLELE AQGDPPSSQF HLMDHPEIPT SALHSLPLSL
SHFSTQFLSP YVLSLTPSMV GDGSKIPVFP NPPTITRFSS SVLSPSLSSH NQTSHYLSNG
GDCESALDLS MGKNSSKSAS SSSSLADKIA AQKGQLLDGL GLRPTSKGLV VVQVKPESVG
VMPSSNSSMS LVNCNNMKKS SIYMRSTEKM NKTLLEREQE KEREKEKERD QDPQQRRAKG
KRYRDMRRSR TIIQAEQLDV LYGCYFKDPN PGKHEFEQIS EWVHLPKKVV QIWFQNMRAR
ERKGEVRFIS DGTLAAVGKP LIKFTWPLSK PIFSNKPPSN NTGCITTAPI VRTLIKTERE
PVKELSKPVM VKKVTPVPIK PKEVVSSTAV SPVSSSVSAV PKTKLETTSN VTMVKVAPKV
NTPVLLAPPK DPIPIAPRPA QKRKLEEESE EEETDEELED EMGPGPGTTN RMVPKLPTTP
INNRPPAATV VPQKQNGLNY WTPKVPIKIN TLSREQLALP THVPPRTIPP PPTPSIAPVS
PNTPSSAKVA SPSPSTPVVA KSSPTESSYL PHSSSRRPRT HLSCLQLSIL QSCYETCAHP
NAMECEAIGT ELNLPLKVVQ IWFQNTRAKE KRWRLQQEKL SPLSGGKVDM SSGSYLQYNA
LKANRPILPK PVQLTITEPA TSPVAGQPVP KETLTGRCDA CNVSFESRAA ARAHVFSPRH
LATLRTTNFG QPTTLVNKNG TGNGGPGSAV PGSQVSHSTP VTSSGGERVI ESPPPTATSN
S
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