ID   TGMH_TACTR              Reviewed;         764 AA.
AC   Q05187;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Hemocyte protein-glutamine gamma-glutamyltransferase;
DE            EC=2.3.2.13;
DE   AltName: Full=Hemocyte transglutaminase;
DE            Short=TGase;
OS   Tachypleus tridentatus (Japanese horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Tachypleus.
OX   NCBI_TaxID=6853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Hemocyte;
RX   PubMed=8093243; DOI=10.1016/s0021-9258(18)54144-2;
RA   Tokunaga F., Muta T., Iwanaga S., Ichinose A., Davie E.W., Kuma K.,
RA   Miyata T.;
RT   "Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and
RT   tissue localization.";
RL   J. Biol. Chem. 268:262-268(1993).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC       of polyamines to proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10024};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in hemocytes, hepatopancreas, and
CC       gastric tissues. On the other hand nothing was detected in the heart,
CC       intestine and muscle.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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DR   EMBL; D12593; BAA02134.1; -; mRNA.
DR   PIR; A45321; A45321.
DR   AlphaFoldDB; Q05187; -.
DR   SMR; Q05187; -.
DR   PRIDE; Q05187; -.
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:UniProtKB-EC.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.90.260.10; -; 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   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; SSF49309; SSF49309; 2.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Calcium; Direct protein sequencing; Membrane;
KW   Metal-binding; Transferase.
FT   CHAIN           1..764
FT                   /note="Hemocyte protein-glutamine gamma-
FT                   glutamyltransferase"
FT                   /id="PRO_0000213717"
FT   ACT_SITE        343
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   BINDING         465
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         527
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   VARIANT         452
FT                   /note="G -> R"
FT   VARIANT         477
FT                   /note="S -> C"
FT   VARIANT         486
FT                   /note="I -> S"
SQ   SEQUENCE   764 AA;  86996 MW;  D4F1D392F1DA5811 CRC64;
     MYGFGRGNMF RNRSTRYRRR PRYRAENYHS YMLDLLENMN EEFGRNWWGT PESHQPDSGP
     SSLQVESVEL YTRDNAREHN TFMYDLVDGT KPVLILRRGQ PFSIAIRFKR NYNPQQDRLK
     LEIGFGQQPL ITKGTLIMLP VSGSDTFTKD KTQWDVRLRQ HDGAVITLEI QIPAAVAVGV
     WKMKIVSQLT SEEQPNVSAV THECKNKTYI LFNPWCKQDS VYMEDEQWRK EYVLSDVGKI
     FTGSFKQPVG RRWIFGQFTD SVLPACMLIL ERSGLDYTAR SNPIKVVRAI SAMVNNIDDE
     GVLEGRWQEP YDDGVAPWMW TGSSAILEKY LKTRGVPVKY GQCWVFAGVA NTVSRALGIP
     SRTVTNYDSA HDTDDTLTID KWFDKNGDKI EDATSDSIWN FHVWNDCWMA RPDLPTGYGG
     WQAYDSTPQE TSEGVYQTGP ASVLAVQRGE IGYMFDSPFV FSEVNADVVH WQEDDSSETG
     YKKLKIDSYR VGRLLLTKKI GVDDDFGDAD AEDITDQYKN KEGTDEERMS VLNAARSSGF
     NYAFNLPSPE KEDVYFNLLD IEKIKIGQPF HVTVNIENQS SETRRVSAVL SASSIYYTGI
     TGRKIKRENG NFSLQPHQKE VLSIEVTPDE YLEKLVDYAM IKLYAIATVK ETQQTWSEED
     DFMVEKPNLE LEIRGNLQVG TAFVLAISLT NPLKRVLDNC FFTIEAPGVT GAFRVTNRDI
     QPEEVAVHTV RLIPQKPGPR KIVATFSSRQ LIQVVGSKQV EVLD