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Database: UniProt
Entry: A0A093F1A3_GAVST
LinkDB: A0A093F1A3_GAVST
Original site: A0A093F1A3_GAVST 
ID   A0A093F1A3_GAVST        Unreviewed;       708 AA.
AC   A0A093F1A3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Transmembrane protease serine 7 {ECO:0000313|EMBL:KFV47929.1};
DE   Flags: Fragment;
GN   ORFNames=N328_06531 {ECO:0000313|EMBL:KFV47929.1};
OS   Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX   NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV47929.1, ECO:0000313|Proteomes:UP000054313};
RN   [1] {ECO:0000313|EMBL:KFV47929.1, ECO:0000313|Proteomes:UP000054313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV47929.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; KK614610; KFV47929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093F1A3; -.
DR   Proteomes; UP000054313; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 3.30.70.960; SEA domain; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF01390; SEA; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Hydrolase {ECO:0000313|EMBL:KFV47929.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KFV47929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KFV47929.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          72..200
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          209..326
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          331..444
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          574..708
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        450..462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        457..475
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        469..484
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        525..537
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        545..560
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV47929.1"
FT   NON_TER         708
FT                   /evidence="ECO:0000313|EMBL:KFV47929.1"
SQ   SEQUENCE   708 AA;  79645 MW;  46A14BC8B9BF00FA CRC64;
     ANISVQTVAA EDKLAKRILA RKKHGKLKLK KKDKLLWNLQ NKIILFTLIL FILGVVTWTL
     LWLFIVQAEN KDALYFVGLF RVANIEFLPE YRQKESKEFL SVAQNVQHVM NLVYTTSSFS
     KFYKQSTVSE VSNNNNGGLL IHFWIVFVVP QAKGQVLCED CVAAILKDSI QTSIINRTSV
     GSLQGLAVDM DSIVLSAGLR SDYWSTTGTG TNCMYDLYAD RLHEHFPLDI HAATEGAICY
     FKLIASVGHL IRLSIVSLQI EADNCITDSL TIYDSLMPIK HKILYRACEP ADSLVSLVST
     NNLMLVMFKA AQIKEQREFH GYFEVITQER CGKAIVTKEK TGYEGRITSP YYPSYYPPKC
     LCAWNFQTPQ KSLGVALKFH NYTISEKNIK GCERGWWKIN EQMYCGYYVD HQTIFHIASS
     AVNIELQCSS EVSEKPLLVE YGSYNISQPC PPGHFKCSTG LCIQQVQRCD GINNCFDESD
     ELFCVVPERN CNSSFTTQDN PLACNGVSDC ENGEDEQNCT HSIPCTSHTF KCRNNICIRK
     QNAKCDGTVD CIDGSDESSC SCGSSRSSNP ISRIVGGMNT EEGEWPWQVS LHFVGAAYCG
     ASVIAKEWLV SAAHCFQGSK LADPRAWRAH LGMQTQGRAK FVSAVRRIIV HEYYNSRNYD
     YDIALLQLSK PWPDTMSQVI QPICVPPFSH KVRSGDKCWI TGWGQKQE
//
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