ID Q3I1X6_PANTR Unreviewed; 684 AA.
AC Q3I1X6; A0A2J8PAM1;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Transglutaminase 4 {ECO:0000313|EMBL:AAZ82262.1, ECO:0000313|Ensembl:ENSPTRP00000074592.1};
DE Flags: Fragment;
GN Name=TGM4 {ECO:0000313|EMBL:AAZ82262.1,
GN ECO:0000313|Ensembl:ENSPTRP00000074592.1,
GN ECO:0000313|VGNC:VGNC:12204};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:AAZ82262.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000074592.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:AAZ82262.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16170411; DOI=10.1371/journal.pgen.0010035;
RA Clark N.L., Swanson W.J.;
RT "Pervasive Adaptive Evolution in Primate Seminal Proteins.";
RL PLoS Genet. 1:E35-E35(2005).
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000074592.1}
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; AACZ04000291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ150486; AAZ82262.1; -; Genomic_DNA.
DR STRING; 9598.ENSPTRP00000074592; -.
DR PaxDb; 9598-ENSPTRP00000025565; -.
DR Ensembl; ENSPTRT00000111381.1; ENSPTRP00000074592.1; ENSPTRG00000014827.7.
DR VGNC; VGNC:12204; TGM4.
DR GeneTree; ENSGT01050000244939; -.
DR OMA; NKEFTCA; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000014827; Expressed in testis.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:SF70; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 4; 1.
DR Pfam; PF00927; Transglut_C; 1.
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:UP000002277}.
FT DOMAIN 260..353
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT NON_TER 684
FT /evidence="ECO:0000313|EMBL:AAZ82262.1"
SQ SEQUENCE 684 AA; 77254 MW; 8F6912F0833768FB CRC64;
MMDASKELQV LHVDFLKQDN AVSHHTWEFQ TSTPVFRRGQ VFHLRLVLNQ PLQSYHQLKL
EFSTGPNPSI AKHTVVVLDL RTPSDHYNWQ ATLQNESGKE VTVAVTSSPN AILGKYQLNV
KTGNHILKSE ENILYLLFNP WCKEDMVFMP DEDERKEYIL NDTGCHYVGA ARSIRYKPWN
FGQFEKNVLD CCISLLTESS LKPTDRRDPV LVCRAMCAMM SFEKGQGVLI GNWTGDYEGG
TAPYKWTGSA PILQQYYNTK QAVCFGQCWV FAGILTTVLR ALGIPARSVT GFDSAHDTER
NLTVDTYVNE NGEKITNMTH DSVWNFHVWT DAWMKRPDLP KGYDGWQAVD ATPQERSQGV
FCCGPSPLTA IRKGDIFIVY DTRFVFSEVN GDRLIWLVKM VNGQEELHVI SMETTSIGKN
ISTKAVGQDR RRDITYEYKY PEGSSEERQV MDHAFLLLSS EREHRRPVKE NFLHMSVQSD
DVLLGNPVNF TVILKRKTAA LQNVNILGSF ELQLYTGKKV AKLCDLNKTS QIQGQVSEVT
LTLDSKTYIN SLAILDDEPV IRGFIIAEIV ESKEIMASEV FTSFQYPEFS IELPNTGRIG
QLLVCNCIFK NTLAIPLTDV KFSLESLGIS SLQTSDHGTV QPGETIQSQI KCTPIKTGPK
KFIVKLSSKQ VKEINAQKIV LITK
//
