ID   G3QUL1_GORGO            Unreviewed;       720 AA.
AC   G3QUL1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Transglutaminase 5 {ECO:0000313|Ensembl:ENSGGOP00000006416.2};
GN   Name=TGM5 {ECO:0000313|Ensembl:ENSGGOP00000006416.2};
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:ENSGGOP00000006416.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000006416.2, 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:ENSGGOP00000006416.2, 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:ENSGGOP00000006416.2}
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   RefSeq; XP_004056118.1; XM_004056070.2.
DR   AlphaFoldDB; G3QUL1; -.
DR   STRING; 9593.ENSGGOP00000006416; -.
DR   Ensembl; ENSGGOT00000006586.3; ENSGGOP00000006416.2; ENSGGOG00000006555.3.
DR   GeneID; 101149000; -.
DR   KEGG; ggo:101149000; -.
DR   CTD; 9333; -.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   OrthoDB; 5344745at2759; -.
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          270..363
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          470..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         400
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         402
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         448
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         453
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   720 AA;  80707 MW;  F0844777DD283C2F CRC64;
     MAQGLEVALT DLQSSRNNVR HHTEEITVDH LLVRRGQAFS LTLYFRNRGF QPGLDNIIFV
     VETGPLPDLA LGTRAVFSLA RHHSPSPWIA WLETNGATST EVSLCAPPTA AVGRYLLKIH
     IDSFQGSVTA YQLGEFILLF NPWCPEDAVY LDSEPQRQEY VMNDYGFIYQ GSKNWIRPCP
     WNYGQFEDKI IDICLKLLDK SLHFQTDPAT DCALRGSPVY VSRVVCAMIN SNDDNGVLNG
     NWSENYTDGA NPAEWTGSVA ILKQWNATGC QPVRYGQCWV FAAVMCTVMR CLGIPTRVIT
     NFDSGHDTDG NLIIDEYYDN TGRILGNKKK DTIWNFHVWN ECWMARKDLP PGYGGWQVLD
     ATPQEMSNGV YCCGPASVRA IKEGEVDLNY DTPFVFSMVN ADCMSWLVQG GKEQKLHQDT
     SSVGNFISTK SIQSDERDDI TENYKYEEGS LQERQVFLKA LQKLKARSFH GSQRGAELQP
     SRPTSLSQDS PRSLHTPSLQ PSDVVQVSLK FKLLDPPNMG QDICFVLLAL NMSSQFKDLK
     VNLSAQSLLH DGSPLSPFWQ DTAFITLSPK EAKTYPCKIS YSQYSQYLST DKLIRISALG
     EEKSSPEKIL VNKIITLSYP SITINVLGAA VVNQPLSIQV IFSNPLSEQV EDCVLTVEGS
     GLFKKQQKVF LGVLKPQHRA SIILETVPFK SGQRQIQANM RSNKFKDIKG YRNVYVDFAL
//