ID W5M1C4_LEPOC Unreviewed; 483 AA.
AC W5M1C4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Ubiquitin-conjugating enzyme E2 variant 3-like {ECO:0000313|Ensembl:ENSLOCP00000002181.1};
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:ENSLOCP00000002181.1, 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:ENSLOCP00000002181.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01008151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015193802.1; XM_015338316.1.
DR RefSeq; XP_015193803.1; XM_015338317.1.
DR AlphaFoldDB; W5M1C4; -.
DR STRING; 7918.ENSLOCP00000002181; -.
DR Ensembl; ENSLOCT00000002187.1; ENSLOCP00000002181.1; ENSLOCG00000001881.1.
DR GeneID; 102684430; -.
DR KEGG; loc:102684430; -.
DR CTD; 55293; -.
DR eggNOG; KOG1495; Eukaryota.
DR eggNOG; KOG2391; Eukaryota.
DR GeneTree; ENSGT00940000153903; -.
DR HOGENOM; CLU_039842_0_1_1; -.
DR InParanoid; W5M1C4; -.
DR OMA; CIMGANG; -.
DR OrthoDB; 5344346at2759; -.
DR Proteomes; UP000018468; Linkage group LG27.
DR Bgee; ENSLOCG00000001881; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006089; P:lactate metabolic process; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF32; UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 3; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR Pfam; PF05743; UEV; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51322; UEV; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 2..145
FT /note="UEV"
FT /evidence="ECO:0000259|PROSITE:PS51322"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52279 MW; F081D9396CF3372E CRC64;
MDLSQESIRK TLGKYKFRDV AIEELQKVHR VNPGFKPLVD TYTFSDSSQK DLLKLVGNIP
VSYQGRSYNL PILLWLLDSF PFTPPICLLR PTPSMMIRVG KHVDARGRIY LPYLHNWDHP
ASSVNGLLSE MIAKFEEEPP LCTKPSADEK DPAELLAYVE KISGGMSTMN IGPPASVGRV
YPERPVNKVT VVGGGDLGVA CLMSILAKGS VDKIVLIDFS EHSSKGGTMD LEIFSLPKVE
VARDLSASAD SKVVVVTSNA WSDDESFVSV VQTNVDLYQG IIPCLARCSP SAVLLIASQP
VDIMTHVAWK QSGLPPSRVI GTGCNLDSER LNYIVSTVLL SRAAGSQPWV VGELSDSKVP
AWSSSAPATD SQPEITPGPT STKPLTDRAF EILKGRGQRS LSVGLSVADI VHSILADQRK
THSVSTLAQG WGGVCGEVFL SLPCELGTGG VARISKLTLG QEEDLKLRNS ATSLRNFIQQ
LRI
//