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Database: UniProt
Entry: A0A3B4WJR3_SERLL
LinkDB: A0A3B4WJR3_SERLL
Original site: A0A3B4WJR3_SERLL 
ID   A0A3B4WJR3_SERLL        Unreviewed;       461 AA.
AC   A0A3B4WJR3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Eva-1 homolog A, regulator of programmed cell death {ECO:0000313|Ensembl:ENSSLDP00000002692.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000002692.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000002692.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the EVA1 family.
CC       {ECO:0000256|ARBA:ARBA00006023}.
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DR   AlphaFoldDB; A0A3B4WJR3; -.
DR   Ensembl; ENSSLDT00000002802.1; ENSSLDP00000002692.1; ENSSLDG00000002152.1.
DR   GeneTree; ENSGT00940000154096; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   CDD; cd22828; Gal_Rha_Lectin_EVA1_EVA1C_rpt1; 1.
DR   Gene3D; 2.60.120.740; -; 2.
DR   InterPro; IPR039500; EVA1_dom.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   PANTHER; PTHR48334:SF1; PROTEIN EVA-1 HOMOLOG A; 1.
DR   PANTHER; PTHR48334; PROTEIN EVA-1 HOMOLOG B-RELATED; 1.
DR   Pfam; PF14851; FAM176; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        342..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..176
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   REGION          236..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  51730 MW;  A6D7EF1A35CA503A CRC64;
     MLQQLLFLLD FLNATERLKN SEASRMFFSD GTLSAVSNAL LLGITCLTVL CDFTKGSSDF
     SGYLSKVLRN YTEQACDGDF LSVRCPPRTT ITVQSAFYGR RGASDFQQCP QTYQALLSSY
     DAREDDRYCS VSTALQKMLD ECQDRRSCQV LVNSRVFGTD QCPGSSKYLI VWYKCRPNEY
     KSKVVCEEER MRLNCKRGMQ IAVYSAMFGR TQQGTLECPL HHRRAPSVVP KKLLQEQGPR
     PPVFSPPPSA HDPNIVGDSP PEGSSVKSPD TVPDKKKIRE TNPNEEKHSE AEKEGGGGEG
     GESLPRPIGM NPIINTTSDS MALISNALAA YTYVSDHPER AALFFVCGVC LGLFLTLFAL
     VVQISCRTDC QPRQRPPAKK RARPADSSSD SSDSDSDWDT TSDLSARRHR RFERTLNMNV
     FTSAEELERA QRLEERERII REIWMNGQPD IPGTRSLNRY Y
//
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