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Database: UniProt
Entry: I3LA49_PIG
LinkDB: I3LA49_PIG
Original site: I3LA49_PIG 
ID   I3LA49_PIG              Unreviewed;       968 AA.
AC   I3LA49;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=HECT and RLD domain containing E3 ubiquitin protein ligase 5 {ECO:0000313|Ensembl:ENSSSCP00000020915.2};
GN   Name=HERC5 {ECO:0000313|Ensembl:ENSSSCP00000020915.2,
GN   ECO:0000313|VGNC:VGNC:88850};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000020915.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000020915.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000020915.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000020915.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; I3LA49; -.
DR   SMR; I3LA49; -.
DR   STRING; 9823.ENSSSCP00000020915; -.
DR   PeptideAtlas; I3LA49; -.
DR   Ensembl; ENSSSCT00000030140.3; ENSSSCP00000020915.2; ENSSSCG00000030548.4.
DR   VGNC; VGNC:88850; HERC5.
DR   GeneTree; ENSGT00940000162703; -.
DR   HOGENOM; CLU_002173_9_2_1; -.
DR   InParanoid; I3LA49; -.
DR   OMA; KHKAYLM; -.
DR   TreeFam; TF315189; -.
DR   Reactome; R-SSC-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-SSC-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Reactome; R-SSC-9833482; PKR-mediated signaling.
DR   Proteomes; UP000008227; Chromosome 8.
DR   Bgee; ENSSSCG00000030548; Expressed in blood and 43 other cell types or tissues.
DR   ExpressionAtlas; I3LA49; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0042296; F:ISG15 transferase activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR   GO; GO:0032020; P:ISG15-protein conjugation; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   PANTHER; PTHR45622:SF7; E3 ISG15--PROTEIN LIGASE HERC5; 1.
DR   PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00415; RCC1; 4.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS00626; RCC1_2; 2.
DR   PROSITE; PS50012; RCC1_3; 4.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:I3LA49};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   REPEAT          101..153
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          154..205
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          206..257
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          259..321
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   DOMAIN          646..968
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        938
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   968 AA;  109448 MW;  4F9B7619B1A5B9D2 CRC64;
     MCCTGGRLAV LERGGAGVEV HQLPAGSDGA RKPKCIKLGK KMKIHSMDQG AEHMLILSSD
     GKPFEYNYSI EHARFQCILQ EKIIIQITCG DYHSLALSKG GELFAWGENL HGQLGVGRGI
     ASTPTPQMVE HLYGVPLAQV SAGGAHSVAL SMSGNVYSWG GNDFGQLGLG HTDDADFPSR
     IEALDGQHVE FLACGASHTA LLTKGGLVLT FGDGRCGQLG HNSTQNELRP RLVTELVGKR
     VTQMACGREH TLAYVSDLGK VFAFGSGTEG QLGNGGTHNQ LIPRPMKLPS NEELKFESRT
     SEKELIMIAG GNQSILLWME KENSYVNLRR KIPTLNEGTV KRWLADVGTK QWQNTKREIR
     EIFSSPACLT GSFLRERITG GRTSVHLDLN TARTALSELA RKDCITNTIT ACLRENLLKA
     LPCHSPHREA VEVFFLLPEC PVMHDDNNWE SLVVPFAEAV GKMSDPSSGV LEEYWASLGE
     SAFIRLVQMF KRAIVAQLRC WTKSAESNCH IKALLELLKK LHRVNQTKCH LPESIFTVNE
     LTDYLDFHED AYRRSFWKVS SDTSVDIQYP VIFSHFPFIF NILSKIKLLY ADSLLKIQQK
     KIRAYMPLAG ILGQEGSELA LPPTLNLLVR RGHLIEDVFS HLSRYENEDL RRELLVSFSG
     EIGYDFGGVR AEFFHCLFEE LTQPEYGLFT YPEDASCMWF PARPKFENKS YFFFGILCGL
     SLFNCNVANI PFPLALFKKL LDQEPSLEDL KELSPVLGQS LQTLLDYEDD DFGKIFHVHF
     NMHWDKDSVD LIPHGSDVIV DQSNKREYIS KYVDYIFNIS VKEVYEEFQR GFYRVCDKEI
     IEFFHPEELK DVIIGNTDYD WETFEKNARY EHGYDNSHPT IVMFWKALHK LTLEEKKKFL
     VFLTGTDRIQ VRGLKNMKIT FCCPENMNEK DPIRAQTCFS VLYLPKYSTM ERVEEALQVA
     ISNHRGFG
//
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