ID H2RL69_TAKRU Unreviewed; 784 AA.
AC H2RL69;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase K {ECO:0000256|ARBA:ARBA00040559};
DE EC=2.3.2.13 {ECO:0000256|ARBA:ARBA00024222};
DE AltName: Full=Epidermal TGase {ECO:0000256|ARBA:ARBA00043229};
DE AltName: Full=Transglutaminase K {ECO:0000256|ARBA:ARBA00041726};
DE AltName: Full=Transglutaminase-1 {ECO:0000256|ARBA:ARBA00041651};
GN Name=TGM1 {ECO:0000313|Ensembl:ENSTRUP00000000882.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000000882.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000000882.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000000882.3}
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 -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000256|ARBA:ARBA00038573}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR AlphaFoldDB; H2RL69; -.
DR STRING; 31033.ENSTRUP00000000882; -.
DR Ensembl; ENSTRUT00000000885.3; ENSTRUP00000000882.3; ENSTRUG00000000379.3.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; H2RL69; -.
DR OMA; WSGNYSD; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000005226; Chromosome 22.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
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:SF49; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE K; 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 Keratinization {ECO:0000256|ARBA:ARBA00023249};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 363..456
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 453
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 784 AA; 86725 MW; 20B9D72760D3961F CRC64;
MPGERLAVRD ASEVGRFPGV APPTRVELTI HKEGEKKEEE GGCRRWLRKA FPCCCQRQNS
ASLDVTDRVE LVAPPTPPLL PEPPKSTPEN GELKEMEEMK LSVCSVDLLS SKTGQNRAEH
HTDMYHGDEL IVRRGQSFQI EVEFNRPFDT DTDKLHLDMR TGPLPTVSKG THATVLLVDS
PEDKRWAAKI VEQSGNKVKL SVNSPASAVC GLYGLTVTCG ATTGEATTTH SCSRNIVVLF
NPWCEEDTVF LDDEEERKEY VLNDTGRIYY GTEKQIGART WNFGQFHEGV LEACLFILEK
SNIPPSGRGD PVNVVRVISA MINAQDDLGV LVGNWSGDYS DGVSPTAWSS SVEILRKYHS
SDGFPVSYGQ CWVFSGVTTT VLRCLGIPAR SVTNFQSAHD TDVSLTTDIY LDENMDPIDY
LNSDSVWNFH VWNDCWMARP DLPPGHGGWQ AVDSTPQETS QGTFRCGPAS ISAIRSGQVF
LKHDTPFVFA EVNSDKIYWQ RNLDGTFSQI YSEKKAVGHY ISTKASGSDE RADITHLYKH
QEGSEEERIA VETASRYGSK PNTYSSPVAE DVSVEVKIDD EGARMGADAQ LSILVKNLSS
HPRRTTLHSQ VAVMYYTGVV KGTIKKEQIS VELQPNEEKT IEWVLPYQQY QNQLVDQAAL
MLTLSGRVNE TQQVLANQTT FRLRTPDITI KPLGEAVVGK EMAAKITFTN PLPRMLVGVV
FRVEGLGLQK GHEVVVGDVG AHSTVTLTEH FIPTQPGPRK LVASLDCKQL TQVHGVADIV
VLEK
//
