ID A0A158NDF3_ATTCE Unreviewed; 690 AA.
AC A0A158NDF3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=105618641 {ECO:0000313|EnsemblMetazoa:XP_012055561.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055561.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012055561.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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}.
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DR EMBL; ADTU01012389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01012390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012055561.1; XM_012200171.1.
DR AlphaFoldDB; A0A158NDF3; -.
DR STRING; 12957.A0A158NDF3; -.
DR EnsemblMetazoa; XM_012200171.1; XP_012055561.1; LOC105618641.
DR GeneID; 105618641; -.
DR KEGG; acep:105618641; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; A0A158NDF3; -.
DR OrthoDB; 3677296at2759; -.
DR Proteomes; UP000005205; 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:InterPro.
DR CDD; cd07066; CRD_FZ; 1.
DR CDD; cd00112; LDLa; 2.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
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; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..208
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 230..355
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 548..690
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 212..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 235..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 243..289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 366..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 404..419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 690 AA; 76882 MW; AD76864434C2007A CRC64;
MTVAMEHKRK SSWDSKISVS TVSTRRFSRA GTPSSILSSD SDIRFTRKLG GQYRCGCCVL
AAFLFFLLFS GVSIYLGYTF LTSDPPGDQV FLATFRVIKG DSFTVELADP STEAFRIRSR
EYRDRLNLIF RRSWLKLSFL ASDVLALDGI EGRDLVVHFD VRFDPRYQTI TSGNIVDILS
RELNPETSRY LTNLTIEAKS LEVQESLKAL NAQSSPQSTV STLPPTTTAP PPRRCSKLDL
SYCKHLPYNI SSYPNMLGHG SLSDVEEDVI AFRELVDAEC YPLAYDFVCQ VLQPACRTSQ
PEDLLELPCR SFCREFWNGC GSRLPEKIKR ALDCSNFPEY IGPSSCRPKP GCVQALQSKA
LSSRICDGVI DCPDLSDEKN CAYCRDGYMH CGVGRTCVPH TKRCDGEADC PNGSDEKDCL
FLASSVHELR SQSWSTPHMA KYNKEGYVVF NEKGTIGKLC TANLNATLPE TEMDNVLQTA
ASSLCTLLTY TGVASVEVRI DDEEDVPYVY MEDPSAPEIT FVRAPCPSKE VLYVRCSDLE
CGIQPLRING GTNGLNKMAE PGDWPWHVAL FKEGVHVCDA TLVADNWLLT TAYCFQGQPK
AEWSARLGVV RLSSTSPWEQ ERRIVGMIKS PVEGTTVLVK LDRPVTTFSD FVRPVCLPSS
EDPPSNTSQC NTLGWARNRM YTIIASYVHK
//
