ID F7EB11_XENTR Unreviewed; 686 AA.
AC F7EB11; A0A6I8SZ55;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Protein-glutamine gamma-glutamyltransferase 4 {ECO:0000313|RefSeq:XP_002937794.2};
DE SubName: Full=Transglutaminase 4 {ECO:0000313|Ensembl:ENSXETP00000018585};
GN Name=tgm4 {ECO:0000313|Ensembl:ENSXETP00000018585,
GN ECO:0000313|RefSeq:XP_002937794.2,
GN ECO:0000313|Xenbase:XB-GENE-1012962};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000018585};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000018585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000018585};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000018585}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002937794.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002937794.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002937794.2};
RG RefSeq;
RL Submitted (SEP-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 RefSeq; XP_002937794.2; XM_002937748.5.
DR PaxDb; 8364-ENSXETP00000024621; -.
DR Ensembl; ENSXETT00000018585; ENSXETP00000018585; ENSXETG00000008494.
DR Ensembl; ENSXETT00000073790; ENSXETP00000100798; ENSXETG00000008494.
DR GeneID; 100488625; -.
DR KEGG; xtr:100488625; -.
DR CTD; 7047; -.
DR Xenbase; XB-GENE-1012962; tgm4.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR HOGENOM; CLU_013435_0_2_1; -.
DR OMA; NKEFTCA; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000008143; Chromosome 6.
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:UP000008143}.
FT DOMAIN 256..349
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 323
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 346
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 686 AA; 76434 MW; BAD96A4EB1F4F320 CRC64;
MALKTEKVDF LKTENTSQHN TNDYDNPNLI LRRGQEFHMK ITFDRELTAN DKVTLQFTTG
SLALPSNGTL VLIDVGPVIQ TNQWSALIRQ RNNKEYLVAV SSPATAIVGK YMLSIITGKG
IVYPLADCTI YLLCNPWCKD DTVYMPSEDG RKEYVLKDTG YIYVGIATKI TAKPWNFGQY
EAEVLDCCMF LLDHGQLKPE HRRDPVILTR KLSALVNSND DRGVLTGNWS GNYSGGFSPT
SWTGSSVILQ KYYKSKRSVM YGQCWVFSGI LTTVLRCLGI PARSVTNFNS AHDTGGNLKV
DVYLNEKGEI LEDLCSDSVW NFHVWNDAWM KRPDLPKGYD GWQAVDATPQ ELSQGVYECG
PCSLAAVKNG DVYLPYDGKF VFAEINADRI CWLVKDKQGD EPPIQIRQEK SCIGECISTK
TVNMNVREDI TVQYKHPEGS PEERETFQKA CSFLNSGACL VSPEPPPYPP AGTKLQIQGD
KELIPGNPLS FTVSIENETN EAKSLDITIG CQLQAYTGKV IASVASIKQS VQVPGKKVAY
IPVTVASEQY MKSVIMVEDE AIFRINAITE NKETQEKTSD SMAIAFTYPP IKVEMPETAK
INEDFSCTFT FKNTLSIQLD KCQLHVEGLS MFKLETFDEG DIKPGGIFRS KIICAPRRPG
EKKIVAKLIS SQIKGISVEK TIIIIN
//