AGSA_APLCA
ID AGSA_APLCA Reviewed; 525 AA.
AC P15287; O96697;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Adenosine deaminase AGSA;
DE EC=3.5.4.4;
DE AltName: Full=Atrial gland-specific antigen;
DE Short=AGSA;
DE AltName: Full=Mollusk-derived growth factor;
DE Short=MDGF;
DE Flags: Precursor;
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Atrial gland;
RX PubMed=2777814; DOI=10.1016/s0021-9258(19)84797-x;
RA Sossin W.S., Kreiner T., Barinaga M., Schilling J., Scheller R.H.;
RT "A dense core vesicle protein is restricted to the cortex of granules in
RT the exocrine atrial gland of Aplysia california.";
RL J. Biol. Chem. 264:16933-16940(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Akalal D.-B.G., Bocangel D.B., Nagle G.T.;
RT "Mollusk-derived growth factor, an Aplysia protein related to insect-
RT derived growth factor.";
RL Abstr. - Soc. Neurosci. 25:168-168(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=14559158; DOI=10.1016/s0169-328x(03)00287-0;
RA Akalal D.B., Bottenstein J.E., Lee S.H., Han J.H., Chang D.J., Kaang B.K.,
RA Nagle G.T.;
RT "Aplysia mollusk-derived growth factor is a mitogen with adenosine
RT deaminase activity and is expressed in the developing central nervous
RT system.";
RL Brain Res. Mol. Brain Res. 117:228-236(2003).
CC -!- FUNCTION: Adenosine deaminase that may contribute to the degradation of
CC extracellular adenosine, a signaling molecule that controls a variety
CC of cellular responses. May play a role in the regulation of cell
CC proliferation. {ECO:0000269|PubMed:14559158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000269|PubMed:14559158};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Dense core vesicles (DCV).
CC -!- TISSUE SPECIFICITY: Detected in egg cordons and in the developiong
CC central nervous system. Not detected in adult central nervous system
CC (at protein level). Atrial gland. {ECO:0000269|PubMed:14559158}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27741.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J05059; AAA27741.1; ALT_FRAME; mRNA.
DR EMBL; AF117336; AAD13112.1; -; mRNA.
DR PIR; A34413; A34413.
DR RefSeq; NP_001191564.1; NM_001204635.1.
DR RefSeq; NP_001191668.1; NM_001204739.1.
DR AlphaFoldDB; P15287; -.
DR SMR; P15287; -.
DR PRIDE; P15287; -.
DR GeneID; 100533339; -.
DR GeneID; 100533516; -.
DR OrthoDB; 430357at2759; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006154; P:adenosine catabolic process; IEA:InterPro.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR013659; A_deaminase_N.
DR InterPro; IPR006331; ADGF.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF08451; A_deaminase_N; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01431; adm_rel; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..525
FT /note="Adenosine deaminase AGSA"
FT /id="PRO_0000006728"
FT ACT_SITE 364
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..163
FT /evidence="ECO:0000250"
FT CONFLICT 4..15
FT /note="FSTHNFVAIATF -> CQRIISCYSNV (in Ref. 1; AAA27741)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="I -> M (in Ref. 1; AAA27741)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> V (in Ref. 1; AAA27741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 60059 MW; CFB518A8F6AD3623 CRC64;
MSSFSTHNFV AIATFVCWFC CLATAAPLTS KAAYLLKRNS LIEEDASRKL GAKIVLTNEE
KVLDDFILAE KRKLIDDSRL NQTEYMPAAS FYRSKDFIDT TFAYKIIQDM PKGGALHLHD
LAIASLDWVV KNATYRDNVY MCMDKDNDVN LRVLQLIPPD PFCVWKLVAT ERANSGDVEA
FDDWLKKNIS YLSTDPVTQY ATVDSVWVRF NKYFAQVIGL LFYAPIMRDY YRQALEEFRA
DNVQYIELRS QLFGFFELDG TVHDAEFGLN LYKSVTEEFQ REYPDFIGAK IILSGLRFKS
QEEILNEVKI AMDLHKKYPD FFLGYDLVGQ EDPNFSLLHY LDALLYPSIQ NPPYRLPYFF
HAAETNWQET EVDYNLADAL LLNTTRVGHG FALIKHPRFT ELAKENGVAV EVNPISNQIL
GLVRDVRNHA LVPLIADDYP IVISSDDPGA WEASPLSHDF YVALMDLCGR DTALTFLKQL
ALNSIRYSAM SDTEKVAAKA KWTTQWDKFV KTSVEGLKPH INDRS
