UniProt: A0A2U9BZP8

Database: UniProt
Entry: A0A2U9BZP8_SCOMX

LinkDB:  A0A2U9BZP8_SCOMX 
Original site:  A0A2U9BZP8_SCOMX

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (3)   
   SMART (4)   
All databases (33)   

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ID   A0A2U9BZP8_SCOMX        Unreviewed;      1710 AA.
AC   A0A2U9BZP8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000256|ARBA:ARBA00018421};
DE            EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
DE   AltName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE   AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN   ORFNames=SMAX5B_014760 {ECO:0000313|EMBL:AWP09774.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09774.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP09774.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC         terminus of a polypeptide.; EC=3.4.19.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000721};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the Toll-like receptor family.
CC       {ECO:0000256|ARBA:ARBA00009634}.
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DR   EMBL; CP026253; AWP09774.1; -; Genomic_DNA.
DR   STRING; 52904.ENSSMAP00000011631; -.
DR   Proteomes; UP000246464; Chromosome 11.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR000157; TIR_dom.
DR   InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR   PANTHER; PTHR47410; TOLL-LIKE RECEPTOR 7-RELATED; 1.
DR   PANTHER; PTHR47410:SF4; TOLL-LIKE RECEPTOR 9; 1.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF01582; TIR; 1.
DR   SMART; SM00364; LRR_BAC; 6.
DR   SMART; SM00365; LRR_SD22; 7.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AWP09774.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1497..1519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1551..1686
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
SQ   SEQUENCE   1710 AA;  193231 MW;  CEB1B47D6E6F91F0 CRC64;
     MESQVMTNPE EVARLYRELS LFPSLNRADV GPVITSQYGG KYSNIYTEWS QRDLGRNDNV
     KFCRQYIVFH DEKSVVFAGT SGNCTEIKGE LISKDSPSGD MKAVVRECSV KGEDKQFLEI
     WSKNIKMKSI DLTALKKHGK VYEDEQFGCL VWSHSETHLL YVAERKRPKA ESFFQTESPE
     LSSIGDEEET MRVEKKEALK GEQFVFREDW GEALVSKNCP VLCVLDIEGD NVSVLEGVPE
     SISPGQAFWA PGDTGVVFVG WWHEPFRLGL KYCPNRRSSL FYVDLTGGKC EQLSSGTSAV
     WSPRLSPDQC RIVYLECSVY GPHMQCSRLC MYDWYTKKTS VVVDVVQRPG EGGFTGIYSS
     QLSPQCWSAD SQRIIVACPQ RSRKDLLMVD IGTGSVTSLT SKCDAGSWCL LNIVRDLMVV
     SCSSPNSPPS LRVGFLPARD SQEEVGWVTL EDSQVLPDIQ CQILTFNPPP EEDNSQYPGL
     DFEALLVKPK EVKDGVKLPL IVIPHGGPHS VIVAEWRLSS SVLCRMGFAI LLVNYRGSLG
     YGQDNILSLC GNVGNQDVKD VQFAVESVLK RGNFDTQKVA VSGGSHGGFL ACHLIGQYPG
     FYKACVACNP VINLASMIGS TDIPDWCMSV IGNNYNMDCL PDPTVWEQML SKSPIKHVAQ
     AMLRNILIIC QLLPFARTRN IKFFPCETDE NVTTVDCYER PIRNIPVITS TTVVSLNLSR
     TKIRQVGQHA FADVPNLLTL KIMGNCQPGQ LRAIKDQSCK MKIHPHAFKS LLSLQSLYLS
     GNSLTSIPWL PETLRVLDLQ NNCIFHITDP LNTPNLEMLF LTKNCFYANP CNQSFYISER
     VFRELRNLKT LTLGHNNLTA VPNGLPPSLE SLDLRENRIT VVSDGAFANL TMLKKLNLEW
     NCQRCDHASR PCFPCPNNHS LYLHPNSFYA ENSSITFLSL RGNSLKTFPE GLFRPLTNLK
     KLDLSDNLLA YAIQNGTFFT ELRGLTWMSL IYNYEPLKTF QELSLSSHIG NISGLQQLLL
     SGNFFHSLSP QSLSVLSKLR HLKTLELRMN FIRNCNLTAL KQLPSLIEID LSQNMLSFLP
     CPSSEILAQH RCQNQNLYTN DFCDQPIIVV DREVTSGDGI WEPNQSKLLE TLKDYVSPFP
     SLWDFRTYFC QNNLTFDLSQ NDILSLNKHV FLGMENAVCL DLSFNYMNQA LRRGQFSSTK
     NLVFLNLSYN RFDLYYTDAF SELKTTLKVL DVSNNDFHFR MRGMGHRFEF LQNLTNLEVL
     SLANNGIGMR IDQMLISSSV KYLYFYGNHL NIMWESGNNQ YTKFFQNLTN LIYLDISDND
     LTSITPDVLC HLPASIESLS ISNNLLNYFP WQNMSALSNL CHLNLSQNYL YYLPYRVIEF
     GANFSLLDLS HNRFSVIPEN FFRKAKSMQY LYLSNNQIKE LDHQYVPTPF KNGSALKILT
     LHANPFKCDC STSWFADFLS TTPVNIPHLT TRIHCEYPES KQGQSILSMD QKSCQDVYGS
     LAFLVCSFLA LTITALPLLK HLYGWDMWYC IQVLWAGHKG YSQLAGSDSH NHYDAFVVFD
     TTNQAVRDWV YNELTVNVEN FGPRRFCLCL EERDWTPGLS CIENLHSAVY NSVKTVFVLS
     SCLNGGETAN GVIRQAFYMV QQRLLDEKGG SVVSPTGGDR VDSASSSCTL ATTIAVAVWA
     ATRLFSSRQQ LAANYEVYIC HWMHRNYARD
//

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