NFXL1_XENLA
ID NFXL1_XENLA Reviewed; 914 AA.
AC A0JMY5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=NF-X1-type zinc finger protein NFXL1;
GN Name=nfxl1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; BC126051; AAI26052.1; -; mRNA.
DR RefSeq; NP_001090441.1; NM_001096972.1.
DR AlphaFoldDB; A0JMY5; -.
DR MaxQB; A0JMY5; -.
DR PRIDE; A0JMY5; -.
DR GeneID; 779353; -.
DR KEGG; xla:779353; -.
DR CTD; 779353; -.
DR Xenbase; XB-GENE-964728; nfxl1.L.
DR OMA; PCPPCAQ; -.
DR OrthoDB; 299100at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 779353; Expressed in blastula and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01422; zf-NF-X1; 10.
DR SMART; SM00438; ZnF_NFX; 11.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..914
FT /note="NF-X1-type zinc finger protein NFXL1"
FT /id="PRO_0000278828"
FT TRANSMEM 892..909
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 163..224
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 269..287
FT /note="NF-X1-type 1"
FT ZN_FING 322..341
FT /note="NF-X1-type 2"
FT ZN_FING 375..394
FT /note="NF-X1-type 3"
FT ZN_FING 428..447
FT /note="NF-X1-type 4"
FT ZN_FING 455..476
FT /note="NF-X1-type 5"
FT ZN_FING 480..499
FT /note="NF-X1-type 6"
FT ZN_FING 507..526
FT /note="NF-X1-type 7"
FT ZN_FING 674..702
FT /note="NF-X1-type 8"
FT ZN_FING 715..733
FT /note="NF-X1-type 9"
FT ZN_FING 777..796
FT /note="NF-X1-type 10"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 830..879
FT /evidence="ECO:0000255"
FT COMPBIAS 18..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 102146 MW; FC0B384F2718B2E1 CRC64;
MDAPWRQAGR GRARGRATSA SGGSSQAPGP VSASNRNASY PRGVPTDGNG VQRPGTGWGN
STYASASKPV TTENVKRETN EENSKKKFEE IQKANQAAVK KLAEDHYSSS DDEDGDEDAD
GKQKKILALT FTSYTSQTDG DLSELARTQQ YVNEAFQAGA VTCLICIASV KRNQAVWSCS
GCFCIFHMPC IQKWAKDSVF LVSSPLTDDD FEKKDYPWPC PKCRYEYKRS ETPCRYYCYC
GKVEDPPLDP WLVPHSCGQV CEREFKPTCG HKCLLLCHPG PCPPCPKMVT ITCFCQKAKP
VPRRCSAKEW SCQQPCRKTL MCKQHKCENP CHKGDCLPCP RVSKQKCLCG RNVAQRPCAS
PTWQCEQVCG KTLPCGNHTC EKICHAGPCG QCPRSGNRLC PCAKSKYTLP CTEDVPTCGD
SCDKLLECAL HKCSQRCHRG PCETCRQEVE KQCRCGKHTK RMPCHKPYLC ETKCAKVRDC
QRHQCKRKCC SGNCPGCDQQ CGRSLGCRNH KCPSVCHRGS CYPCPETIDV KCNCSKTVLK
VPCGRERTTK PPKCKEVCSC PSTCHHEARE RHRCHFGPCP PCRQTCKKIL NRCSHLCPVP
CHDEALVKQK GLPQPAGPWE QPSEPTFIQT ALPCPPCQVP IPTECLGKHE ISPLPCHAAG
PFSCKRPCGR PLACGNHTCS RECHKVTDVN GNKERAGVEC AACEEECNKP RPPECPHRCN
LPCHSDDCPP CVQMIRTKCH CKISNLFIEC TKLSMADAKE KNNLTSCKNQ CPKELPCGHR
CKEICHQGNC SLNCIQKVKL RCPCRRIKKE MPCNSVREGH ISLECDSVCL DVRKKAAEMK
AEEENAAVEQ ERRRQQAELE AFENRLKGKR RKNKRKDEVE VQQTAWQKYK KYIMMPVCGI
ALAVFTLYYT QVDV