ID G3SA72_GORGO Unreviewed; 718 AA.
AC G3SA72;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Transglutaminase 5 {ECO:0000313|Ensembl:ENSGGOP00000024994.2};
GN Name=TGM5 {ECO:0000313|Ensembl:ENSGGOP00000024994.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000024994.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000024994.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000024994.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000024994.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR EMBL; CABD030095854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3SA72; -.
DR Ensembl; ENSGGOT00000028725.2; ENSGGOP00000024994.2; ENSGGOG00000006555.3.
DR eggNOG; ENOG502QTRA; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000001519; Chromosome 15.
DR Bgee; ENSGGOG00000006555; Expressed in heart.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR PANTHER; PTHR11590:SF38; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 5; 1.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 268..361
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 468..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 358
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 718 AA; 80629 MW; 941B850E7D4DFDFB CRC64;
MAQDVSRGWN FSSRNNVRHH TEEITVDHLL VRRGQAFSLT LYFRNRGFQP GLDNIIFVVE
TGPLPDLALG TRAVFSLARH HSPSPWIAWL ETNGATSTEV SLCAPPTAAV GRYLLKIHID
SFQGSVTAYQ LGEFILLFNP WCPEDAVYLD SEPQRQEYVM NDYGFIYQGS KNWIRPCPWN
YGQFEDKIID ICLKLLDKSL HFQTDPATDC ALRGSPVYVS RVVCAMINSN DDNGVLNGNW
SENYTDGANP AEWTGSVAIL KQWNATGCQP VRYGQCWVFA AVMCTVMRCL GIPTRVITNF
DSGHDTDGNL IIDEYYDNTG RILGNKKKDT IWNFHVWNEC WMARKDLPPG YGGWQVLDAT
PQEMSNGVYC CGPASVRAIK EGEVDLNYDT PFVFSMVNAD CMSWLVQGGK EQKLHQDTSS
VGNFISTKSI QSDERDDITE NYKYEEGSLQ ERQVFLKALQ KLKARSFHGS QRGAELQPSR
PTSLSQDSPR SLHTPSLQPS DVVQVSLKFK LLDPPNMGQD ICFVLLALNM SSQFKDLKVN
LSAQSLLHDG SPLSPFWQDT AFITLSPKEA KTYPCKISYS QYSQYLSTDK LIRISALGEE
KSSPEKILVN KIITLSYPSI TINVLGAAVV NQPLSIQVIF SNPLSEQVED CVLTVEGSGL
FKKQQKVFLG VLKPQHRASI ILETVPFKSG QRQIQANMRS NKFKDIKGYR NVYVDFAL
//
