ID   A0A3B3X9L6_9TELE        Unreviewed;       453 AA.
AC   A0A3B3X9L6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000011732.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000011732.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   RefSeq; XP_014860596.1; XM_015005110.1.
DR   AlphaFoldDB; A0A3B3X9L6; -.
DR   STRING; 48701.ENSPMEP00000011732; -.
DR   Ensembl; ENSPMET00000018955.1; ENSPMEP00000011732.1; ENSPMEG00000013843.1.
DR   GeneID; 106928674; -.
DR   KEGG; pmei:106928674; -.
DR   CTD; 777630; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF14; TRANSMEMBRANE PROTEASE SERINE 3-LIKE; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..214
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          223..450
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        90..105
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   453 AA;  49294 MW;  A7B8628323D39267 CRC64;
     MGASQTSFQE AADIDIPLNS NMPNAQQKPM ANSKPQAAKM SRTKKIIWIL MAVVILAILV
     IAGYFIKKLI ETHYYYCTRS AKFIPLAKSC DGHADCYDGE DEAYCTSEFK ANGTFPVRLI
     SAASVLQVFN GKTWRTVCND DWTAQHTETT CKQLGYTKSP TSKSVDVSTL QYSLKTGPFA
     AVWSGSGSTP VHQATTDRSV CRTGSVVSLM CSDCGQVNSV DRIVGGVDAH IEDYPWQVSL
     HNGGHRCGGS LVSARWIVTA AHCFTNNKEV SRWTVMSGET FMSAFGTSSV DKIIIHDQYN
     TDTNDYDLAM MRLSSPISVG DKRKPVCLPP KDLPLPYKAP VVVTGWGLLR ENGKTATRLQ
     MANIEIISRN TCSGIYGSSL SQRMICAGIL AGGVDSCQGD SGGPLVYLSS SSQWNLVGVV
     SWGDGCARQN RPGVYSNVDD MLNWIYTVIE KNS
//