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Database: UniProt
Entry: W5MF94_LEPOC
LinkDB: W5MF94_LEPOC
Original site: W5MF94_LEPOC 
ID   W5MF94_LEPOC            Unreviewed;       317 AA.
AC   W5MF94;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Si:dkey-23c22.5 {ECO:0000313|Ensembl:ENSLOCP00000007053.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007053.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000007053.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00206}.
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DR   EMBL; AHAT01009808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01009809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01009810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MF94; -.
DR   STRING; 7918.ENSLOCP00000007053; -.
DR   Ensembl; ENSLOCT00000007061.1; ENSLOCP00000007053.1; ENSLOCG00000005841.1.
DR   eggNOG; ENOG502S1XZ; Eukaryota.
DR   GeneTree; ENSGT00950000183126; -.
DR   HOGENOM; CLU_076255_0_0_1; -.
DR   InParanoid; W5MF94; -.
DR   OMA; PGMYCKS; -.
DR   Proteomes; UP000018468; Linkage group LG25.
DR   Bgee; ENSLOCG00000005841; Expressed in zone of skin and 13 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0046642; P:negative regulation of alpha-beta T cell proliferation; IBA:GO_Central.
DR   GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IBA:GO_Central.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IBA:GO_Central.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13405; TNFRSF14_teleost; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 5.
DR   InterPro; IPR008063; Fas_rcpt.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   PANTHER; PTHR46838; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 14; 1.
DR   PANTHER; PTHR46838:SF1; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 14; 1.
DR   Pfam; PF00020; TNFR_c6; 4.
DR   PRINTS; PR01680; TNFACTORR6.
DR   SMART; SM00208; TNFR; 6.
DR   SUPFAM; SSF57586; TNF receptor-like; 5.
DR   PROSITE; PS00652; TNFR_NGFR_1; 3.
DR   PROSITE; PS50050; TNFR_NGFR_2; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00206};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..38
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          4..38
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   REPEAT          40..82
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          40..82
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          106..146
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          106..146
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          148..190
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          148..190
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   DISULFID        17..30
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        20..38
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        41..56
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        125..138
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        128..146
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        149..164
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
SQ   SEQUENCE   317 AA;  34593 MW;  B572208A453E8E2A CRC64;
     MCEACDSQEY AHGEICCPKC NRGERVAKNC TDTTSTLCKT CPESTYMDHP NELNECKRCQ
     KCEAEEGMIT KLRCSPTSNS VCECGEGFFC SVPADRGCSK CLNHTVCSEG QFTKQNEYLV
     NGECCPMCPI GSRVLRHCTE FSNTSCIPCV GPTYTDQPNG LLSCFPCKVC DPGLGLRTLH
     GCTNQKDTVC WVLSGYYCID QADGGCRAAR PHTVCAPGQW VKQPGSDSTD TECEDCPQNS
     YSDGLFTSCK PHTDCEARGL QEIRPGTSAS DVECGEMSNP VVPIVTVLAI FIPISIRVVI
     FLVLKKKIPF LKGKVKQ
//
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