ID A0A401S2I3_CHIPU Unreviewed; 917 AA.
AC A0A401S2I3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=chiPu_0002951 {ECO:0000313|EMBL:GCC24549.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC24549.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC24549.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC24549.1}.
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DR EMBL; BEZZ01000060; GCC24549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S2I3; -.
DR STRING; 137246.A0A401S2I3; -.
DR OMA; YLEAFSY; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF31; AMINOPEPTIDASE Q; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW ECO:0000256|RuleBase:RU364040};
KW Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 83..270
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 267..499
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 571..888
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 45..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 432
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 917 AA; 106326 MW; AC368F4BFDD400D9 CRC64;
MGPKSNSGFY LSKKAAVFFA FLVLALLVIL TVFVGLYAKL RAERTQEVTP ATREPPSVSS
SMQPGAERLG PWNHTRLPSN LQPIYYQLEL WPKQVHPGKD HLYFLIGQAN VTVMCLEETE
VFLIHSRNLN YSGLSLTAGA HSPQLDPRPV PNIQEIWLEV SHDYLVIELD GKLVPGQQYI
LQSNYSGQLD EKLQGLFIIP DPEKEHQKPI IASLLEPTFA RSVFPCFDEP AMKATFDIRL
VNRPEFVAIS NMPAIDKTAI SNGEAEYALN ITGPILAYFE KYYDVNYPLP KIDIVALPLY
GPEAMENWGL LLFRKSSLLL DPKKESFKKL AITAVIAHEL AHQARLYNWF GNLATIRWWN
NLWLNEGFAS YFENLEFSSE DHVKKWKHRY PIHLKYFVFQ SEENIFSHSL SMKKEDIETF
DEIMEMFSDT TYIKGASVID MISHFMTEEL FSKGLTSYLK AFSYSNAEAD DVWNHLQMAI
DSQDVIKLPT SIKSIMDTWT MQEGLPIITV NTTSGTVKQD YFGKSKENRN SNYSWFIPIF
WMKNGSMQPL IWFDGESKTY PEIKRTTDEE WILLNINVST LCRIVYDDSN WQQLILQLNK
DPTVIPSSNR MQLICDAFDL EKIGNINIRT ALSTTTYLAK EQDNDVWYAA FHYFSRLEKV
IRTTYTFGLY KKYIFSRIVP FYYHQMKLMN EDFNNIHNSS VEKTIFLKTL NKLYLLDLKD
LMDRATDLYS QLMSNPANNT IPSYARRHIY CEAIKAGSEK EWNFAWSLYQ NSSQDDEVLL
FAMGCSREPW ILSRYLHYTL DELIVSEKHS YTVYQSVAEN PIGWALAWNF LRANWNSINT
NSTYYFELMT LLDTVSEGLL TDFGLQEFEL FLNSTTDEEE WAHTVQQLII DSRDLLNWNK
KIHTEVHNWL SEHIPAN
//
