ID G3STP9_LOXAF Unreviewed; 1101 AA.
AC G3STP9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Activity dependent neuroprotector homeobox {ECO:0000313|Ensembl:ENSLAFP00000003451.1};
GN Name=ADNP {ECO:0000313|Ensembl:ENSLAFP00000003451.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003451.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003451.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003451.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003451.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003451.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
CC ECO:0000256|RuleBase:RU000682}.
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DR RefSeq; XP_003419943.1; XM_003419895.2.
DR RefSeq; XP_010597735.1; XM_010599433.1.
DR AlphaFoldDB; G3STP9; -.
DR STRING; 9785.ENSLAFP00000003451; -.
DR Ensembl; ENSLAFT00000004139.1; ENSLAFP00000003451.1; ENSLAFG00000004139.1.
DR GeneID; 100661948; -.
DR KEGG; lav:100661948; -.
DR CTD; 23394; -.
DR eggNOG; ENOG502QSYX; Eukaryota.
DR GeneTree; ENSGT00530000063631; -.
DR HOGENOM; CLU_009119_0_0_1; -.
DR InParanoid; G3STP9; -.
DR OMA; PYCTFNG; -.
DR OrthoDB; 4079234at2759; -.
DR TreeFam; TF328818; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR038861; ADNP/ADNP2.
DR InterPro; IPR045762; ADNP_Znf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15740:SF1; ACTIVITY-DEPENDENT NEUROPROTECTOR HOMEOBOX PROTEIN; 1.
DR PANTHER; PTHR15740; NEUROPROTECTIVE PEPTIDE-CONTAINING PROTEIN; 1.
DR Pfam; PF19627; ADNP_N; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 512..540
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 770..813
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 772..814
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 354..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 123466 MW; E1B832B9371E8718 CRC64;
MFQLPVNNLG SLRKARKTVK KILSDIGLEY CKEHIEDFKQ FEPNDFYLKN TTWEDVGLWD
PSLTKNQDYR TKPFCCSACP FSSKFFSAYK SHFRNVHSED FENRILLNCP YCTFNADKKT
LETHIKIFHA PNASAPSSSL STFKDKNKND GLKPKQADSV EQAVYYCKKC TYRDPLYEIV
RKHIYREHFQ HVAAPYIAKA GEKSLNGAVP LGSNAREECG IHCKRCLFMP KSYEALVQHV
IEDHERIGYQ VTAMIGHTNV VVPRSKPLML IAPKPQEKKG MGLPPRISSL ASGNVRSLPS
QQMVNRLSIP KPNLNSTGVN MMSNVHLQQN NYGVKSVGQG YGVGQSMRLG LGGNAPVSIP
QQSQSVKQLL PSGNGRSYGL GSEQRSQAPA RYSLQPANAS SLPSGQLKSP SLSQSQASRV
LGQSSSKPTA AATGPPPANT SSTQKWKICT ICNELFPENV YSVHFEKEHK AEKVPAVANY
IMKIHNFTSK CLYCNRYLPT DTLLNHMLIH GLSCPYCRST FNDVEKMAAH MRMVHIDEEM
GPKTDSTLSF DLTLQQGSHT NIHLLVTTYN LRDAPAESVA YHAQNTPPVP PKPQPKVQEK
ADVPVKSSPQ AAVPYKKDVG KTLCPLCFSI LKGPISDALA HHLRERHQVI QTVHPVEKKL
TYKCIHCLGV YTSNMTASTI TLHLVHCRGV GKTQNGQDKT NAPSRLNQSP GLAPVKRTYE
QMEFPLLKKR KLDEDVDSPA FEEKPEEPVV LALDPKGHED DSYEARKSFL TKYFNKQPYP
TRREIEKLAA SLWLWKSDIA SHFSNKRKKC VRDCEKYKPG VLLGFNMKEL NKVKHEMDFD
AEWLFENHDE KDSRVNASKT ADKKLNLGKE DDSSSDSFEN LEEESNGSGS PFDPVFEVEP
KLPTDNPEEH IPKVIPEDDL EAEEKLDQKE ENSSKYETIH LTEEPTKLLH DASDSEVDQD
DVEWKDGASP SESGPGSQQV SDFEDNTCEM KPGTWSDESS QSEDARSSKP AAQKKATMQG
DREQLKWKNS SYGKVEGFWS KDQSQWKNAS ENDERLSNPQ IEWQNSTIDS EDGEQFDTMT
DGVAEPMHGS LTGVKLSSQQ A
//
