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Database: UniProt
Entry: A0A1A9W2G5_9MUSC
LinkDB: A0A1A9W2G5_9MUSC
Original site: A0A1A9W2G5_9MUSC 
ID   A0A1A9W2G5_9MUSC        Unreviewed;       899 AA.
AC   A0A1A9W2G5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Peptidase M28 domain-containing protein {ECO:0000259|Pfam:PF04389};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI003962-PA, ECO:0000313|Proteomes:UP000091820};
RN   [1] {ECO:0000313|Proteomes:UP000091820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GBRI003962-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI003962-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|ARBA:ARBA00010918}.
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DR   AlphaFoldDB; A0A1A9W2G5; -.
DR   STRING; 37001.A0A1A9W2G5; -.
DR   EnsemblMetazoa; GBRI003962-RA; GBRI003962-PA; GBRI003962.
DR   VEuPathDB; VectorBase:GBRI003962; -.
DR   OrthoDB; 277019at2759; -.
DR   Proteomes; UP000091820; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03875; M28_Fxna_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR048024; Fxna-like_M28_dom.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        407..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        516..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        570..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        614..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        643..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..367
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   899 AA;  102225 MW;  3CF4C1E44CD29C3D CRC64;
     MQLDKTPSSL HSLLRSRKRR ELKIWDGEEE EEDEMLIVEP KPRRVFHLTE EKSARISLKC
     APFFIAFWAV LYLAIVRTQI TNLPKPLYRA DEHSNPESFI AERAEITLIN LTSIGPRVVG
     SIANEVTAIK FLLNEIGKIR KEASDFFEFE VEIQEATGNY VHWSMINMYQ SIQNVIIKIS
     AKNSNSENYV LINSHYDTVP TSPGAGDDGS MVAIMLEVMR VISKSKGPLE HPIVFLFNGA
     EENPLQASHA FITQHKWAKN CKALINLDAA GNGGREILFQ SGPQHPWLMK YYRQVSHPFA
     TCSAEEIFQA GLIPSDTDFR IFRDFGGVPG YDMAFITNGY VYHTEHDKVN VLPKGSLQHT
     GDNVLTLAKC LANAQELNDS SQHSEGHVVF FDFLGSFMIF YTESVGIILN IIVCLIAIIA
     IGLSLYLMAV DSAISLKSML SSFAASFAVQ VATLVAAGGL AFLNALFIDA IGSAMSWYSQ
     KWIFMGLYFC PLFFAMGFLP ACYLSKSRKG KLYLGFHIQL LMHSHCLFLI VVTIVLTCFG
     IRSAYMLMMA VLFYALALII NLITKCYRSV YWFALIMTVC QILPFLYYTS LTHIIYDAMV
     PMAGRSGSSS NPEIFMCGIA IFFTILFAGF IISLLQFFQK ARVLFTTFLI VALVFIIIAL
     TPLGFPYKDK TASQRHALIH AHRIIHDADK TIRVKESGIY VFPQDRNVKI LNEHIESIGQ
     RHTVSDYCDK EMFCGMPFYN HRWYKARDFS FWIPIEEDPH IPDEPPILNL LSSNQFTDPF
     KTNYEFELSG PDHMTIFIGV KGQGRILDWS FNDTMIRENW EPPYFIYFSW GTNRAALKFT
     ILVEKTAETL NKPILEIGIG GHWTHNEKSR PRKYQQFVNS LPDYSTLTDW VATYESWIF
//
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