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Database: UniProt
Entry: A0A0Q3U3J5_AMAAE
LinkDB: A0A0Q3U3J5_AMAAE
Original site: A0A0Q3U3J5_AMAAE 
ID   A0A0Q3U3J5_AMAAE        Unreviewed;      1461 AA.
AC   A0A0Q3U3J5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Transmembrane protease serine 7 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AAES_07323 {ECO:0000313|EMBL:KQL60438.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL60438.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQL60438.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQL60438.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:KQL60438.1}.
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DR   EMBL; LMAW01000146; KQL60438.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3U3J5; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 3.30.70.960; SEA domain; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 4.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR003096; SM22_calponin.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   PANTHER; PTHR24253:SF103; TRANSMEMBRANE PROTEASE SERINE 7; 1.
DR   Pfam; PF00402; Calponin; 1.
DR   Pfam; PF00431; CUB; 3.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF01390; SEA; 2.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   PRINTS; PR00890; TRANSGELIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00020; Tryp_SPc; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 3.
DR   SUPFAM; SSF82671; SEA domain; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 4.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS01180; CUB; 4.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS50024; SEA; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..336
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          345..462
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          467..580
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          710..944
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          963..1087
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          1084..1199
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          1165..1461
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          1204..1269
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DISULFID        586..598
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        593..611
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        605..620
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        640..655
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        661..673
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        681..696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1461 AA;  162890 MW;  83A3338532395BD4 CRC64;
     MAAVQRTLMA LGSLAVTKDD GCYKGDPSWF HRKAQQNRRG FSEEQLRQGQ NVIGLQMGSN
     KGASQSEYGN QTMEDGNSWI SLFTCNVTVV RCELPTEHGV GNKACKELSC SDHDCCHQGS
     RISVVPLVSA FIYSQVANIS VQMVAAEDKL AKRILARKKH GKLKLKKKES LLWNFQNKII
     LFTLILFILG VVTWTLLWLF IVQAENKDAL YFVGLFRVAN IEFLPEYRQK ESKEFLSVAK
     NVQHVMNLVY TTSSFSKFYR QTTVSEVSNN NNGGLLVHFW IIFVVPQAKG QVLCEDCVAA
     ILKDSIQTST TNRTSVGSLQ GLAVDMDSIV LSAGLRSDYW SSTGTGTNCM YDMYADRLHE
     RFPLDILTTS GSTICYFKLT ASVGHLIRLS IVSLHIEADN CITDSLTIYD SLMPIAHKIL
     YQACEPADSS VSLVSTNNLM LVMFKAAQIK EQKEFHGYLE VITQERCGKA IITKEKIGYE
     GRITSPYYPS YYPPKCLCAW NFQTPQKSLG IALKFHNYTI SEKNIKGCER GWWKINEHMY
     CGXYVDHQTV FHIASSAVSI ELQCSSKVSE KPLLVEYGSY NISQPCPPGH FKCSTGLCIQ
     QMQRCDGINN CFDESDELFC AVPEWNCNSS FTIQDSPLAC DGVSDCENGK DEQNCTHSIP
     CTNHTFQCRN NICIRKQNAK CDGTVDCIDG SDESSCSCGS SKSNNPNSRI VGGTNTQEGE
     WPWQVSLHFV GAAYCGASVI SKEWLVSAAH CFQGSKLADP RAWSAHLGMQ IQGHAKFVSA
     VRRIIVHEYY NSRNYDYDIA LLQLSKPWPD TMSHVIQPIC VPPFSHKARS GDKCWITGWG
     QKQEADDQGS AVLQKAEVKI IDQTVCHSTY GVITARMFCA GLMSGKRDGC KGDSGGPLSC
     QSNGDGKWFL TGIVSWGYGC GRPNFPGVYT RVSNFAPWIY KYVPSVLSAG SGFKQYGKAP
     AFSFIYIGGS VEIPNVTYXS DFNDPKSQKF LLQAEAIQNY FAETYESSFL GKYYLKSVVA
     AFSEGESGLR AFYWNTFWAP QDVVASFKSL TPVEMKGISA KQAAHMFSSS GEEHFDLATM
     ELFASFDLYA KPGNNRTLTL VNPKKSFYQW RLRVPSNYVV RLVVITLHGV TPESCASHHX
     SAYDFLLPLQ NKIITRWCGP GGWTPPIVRL TSSSNVMLLT FSLDRREESS ILKAHFQAVP
     KIMCGGHYIS WNGTLSSPYY PSYYPPNIDC SWIIRAPLPG YKLSLKILII QIQEESPGSS
     KCDKDWLEID GVRYSIPSGW RAYMGLHTIT EKSNRVAMRS IKRIVVHPQY DHSISDYDIA
     LLEMETPVFF SELVQPICLP STSRVFVYGT VCYVTGWGAI KENSHLAKTL QEARVRIINX
     SVCNKLYXNL ITXRMLCAGN LNGGVDACQG DSGGPLACMG KGNRWYLAGI VSWGEGCARR
     NRPGVYTKVT ALYDWIRQTT S
//
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