ID A0A091EHH6_FUKDA Unreviewed; 1423 AA.
AC A0A091EHH6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Puromycin-sensitive aminopeptidase {ECO:0000313|EMBL:KFO34916.1};
GN ORFNames=H920_03618 {ECO:0000313|EMBL:KFO34916.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34916.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO34916.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO34916.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; KN121896; KFO34916.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000000963; -.
DR MEROPS; M01.010; -.
DR eggNOG; KOG1046; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR017978; GPCR_3_C.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00003; 7tm_3; 2.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 2.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KFO34916.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..308
FT /note="G-protein coupled receptors family 3 profile"
FT /evidence="ECO:0000259|PROSITE:PS50259"
FT DOMAIN 323..421
FT /note="G-protein coupled receptors family 3 profile"
FT /evidence="ECO:0000259|PROSITE:PS50259"
FT REGION 497..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 884
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 883
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 969
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1423 AA; 159454 MW; 1C301455BEC23766 CRC64;
MPPQGIRAAL AFLYSGDAQQ LLRANCSQRY EVPGVEARPG RPPVLQRAAG ALAQAANLLN
VLLQANDIRE ASVEEDAEWY QALVRSVAEG DPRARRVRLT FNSPPGASSP PLALQATRMG
AETLLQQLAG SRVGEASAAE GPDAAALHRR VLTNDLRSLG SPKWPRGDAY MGDMQQVRLS
PPFLDCQEGQ LRPGWLVTLS ATFYGLTPDL SPEVRGQVQM DVDLQSVDIN QCANGPGWFS
DTHLCDLNST QRIRVSGVVL LEAILFGSLL LYFSVFILCF KPSVFRCIAL RWVRLLGFAM
VYGTIILKLY SHNPQALQVV EVLLLCWGNF LSSTTRVVPS AFHEPRYLGL ALRNELLLST
AFHLARFMLV PSLHPDWTLL LFFFHTHSTV TTTLALIFVP KLQKPGLPPH EEILEEVDED
ELDLQRSGSY LDSSIASAWS GRSLDPGDIR DELKKLYAQL EVRKTKEMAA NNPHLPRKRG
SSRQRLGRSF MRLLSSSHQD APDGALHQSR RAYDQHHREQ ELPLLGSMLR RTLSRKASRP
EGWEPTPGLP TLGFRSASAH NLTVGERLPQ AWPGFLHKSL SVMASSREKA LLVASQAYLE
ETYWQVKERQ ERQRAEVRQA TNQIVMNCAD IDIITASYAP EGDEEIHATG FNYQNEDEKV
TLSFPSTLQT GTGTLKIDFV GELNDKMKGF YRSKYTTPSG EVRYAAVTQF EATDARRAFP
CWDEPAIKAT FDISLVVPKD RVALSNMNVI DRKPYPDDEN LVEVKFARTP VMSTYLVAFV
VGEYDFVETR SKDGVCVRVY TPVGKAEQGK FALEVAAKTL PFYKDYFNVP YPLPKIDLIA
IADFAAGAME NWGLVTYRET ALLIDPKNSC SSSRQWVALV VGHELAHQWF GNLVTMEWWT
HLWLNEGFAS WIEYLCVDHC FPEYDIWTQF VSADYTRAQE LDALDNSHPI EVSVGHPSEV
DEIFDAISYS KGASVIRMLH DYIGDKDFKK GMNMYLTKFQ QKNAATEDLW ESLENASGKP
IAAVMSTWTR QMGFPLIYVE AEQVEDDRLL RFSQKKFCAS GPYVGEDCPQ WMVPITISTS
EDPHQAKLKI LMDKPEMSVV LKNIKPDQWV KLNLGTVGFY RTQYSSAMLE SLLPGIRDLS
LPPVDRLGLQ NDLFSLARAG IISTVEVLKV MEAFVNEPNY TVWSDLSCNL GILSTLLSHT
DFYEEIQEFV KDVFSPIGER LGWDPKPGEG HLDALLRGLV LGKLGKAGHK ATLEEARRRF
KDHVEGKQVL SADLRSPVYL TVLKHGDGAT LDVMLKLHKQ ADMQEEKNRI ERVLGATLMP
ELIQKVLTFA LSEEVRPQDT VSVIGGVAGG SKHGRKAAWK FIKDNWEELY NRYQGGFLIS
RLIKLSVEGF AVDKMAGEVK VREALSTSHF AVSAHKWCPL AFS
//
