ID A0A3Q1J2Q3_ANATE Unreviewed; 877 AA.
AC A0A3Q1J2Q3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Endothelial PAS domain protein 1b {ECO:0000313|Ensembl:ENSATEP00000025659.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025659.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025659.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A3Q1J2Q3; -.
DR Ensembl; ENSATET00000026077.2; ENSATEP00000025659.1; ENSATEG00000017802.2.
DR GeneTree; ENSGT00940000155930; -.
DR OMA; SGPNEKP; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd19728; bHLH-PAS_HIF2a_PASD2; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR014887; HIF-1_CTAD.
DR InterPro; IPR021537; HIF_alpha-like.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR23043:SF8; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR Pfam; PF11413; HIF-1; 1.
DR Pfam; PF08778; HIF-1a_CTAD; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 14..67
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 91..153
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 248..299
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 398
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT MOD_RES 538
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
FT MOD_RES 854
FT /note="(3S)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR621537-50"
SQ SEQUENCE 877 AA; 97042 MW; EFB64FE5053FA83E CRC64;
MTAEKDKKRS SSERRKEKSR DAARCRRSKE TEVFYELAHQ LPLPHSISSH LDKASIMRLA
ISFLRTRKLL ATGCRSSSDS DEDRQMDSLY LKSLEGFITV VTSDGDMIFL SENINKFMGL
TQVELTGHSI FDFTHPCDHE EIRENLSLKT AGSSFGKKGK ELSTERDFFM RMKCTVTNRG
RTVNLKSASW KVLHCTGHLK MYNGCPPRVL CGFKEPPLTC AVLMCEPIPH PSNIDTPLDS
KTFLSRHSMD MKFTYCDERV TELMGYTPED LLGRSVYDFY HALDSDSVTK SHHNLCTKGQ
AVSGQYRMLA KNGGYVWVET QGTVIYNSRN SQPQCIVCIN YVLSDIEEKS LIFSLEQTES
LFKPHHMSSF FTGLTGESGD ALFTKLKEEP EDLAQLAPTP GDTIISLDFG HPEFDEPQQP
AGYTQVSTEA MLPPGPPSWA SKSHKPVPPA SGQTPAPGDI TNMASPFTVQ QNLPPGSATP
SLSSCSTPSS PGDYYSSVES DLKVELTEKL FALDTEGHNS PANTERDLSD LDLETLAPYI
PMDGEDFQLN PIMPESEPME AGSAGSIGSS NNSLPKSHRA TPQSFSNIAS LFQPLSSSSQ
PQPHYQPQQA TTWASGEKRS SSQRNIDCRA ESYMMGRMQN PPYQAPASTP LSSMGGRQNL
QWPPDPLLTY QQQPGVTKAY LMDTLSGDER PSCQQNMTHL MQKQRSIDNF VQAYRDMSPA
RVAMANSIKR SFTQMSVTES KPSEIMWKKM RGDSCVTIDR SLSAGSLADS GMSRMTPGSM
SSCLSSLQQH RKSQHPGNGI GVANEKGFPQ KSCNYTEYNM LPSNKTEGIA SRLLGPSFEP
SCLPELTRYD CEVNVPLQGN LHLLQGCDLL RALDQAT
//
