ID A0A401PFI0_SCYTO Unreviewed; 1675 AA.
AC A0A401PFI0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Transmembrane protease serine 7 {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0008954 {ECO:0000313|EMBL:GCB71854.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB71854.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB71854.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
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:GCB71854.1}.
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DR EMBL; BFAA01003539; GCB71854.1; -; Genomic_DNA.
DR STRING; 75743.A0A401PFI0; -.
DR Proteomes; UP000288216; 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; 3.
DR CDD; cd00112; LDLa; 5.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
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; 4.
DR InterPro; IPR000859; CUB_dom.
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; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 5.
DR Pfam; PF01390; SEA; 2.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 3.
DR SMART; SM00192; LDLa; 6.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
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; 3.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 5.
DR PROSITE; PS50024; SEA; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 4: Predicted;
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:UP000288216};
KW Serine protease {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 779..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..209
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 218..336
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 580..912
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 934..1062
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1075..1191
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1196..1305
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1437..1675
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 460..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 467..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 479..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 533..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 553..568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1317..1335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1329..1344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1350..1368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1362..1377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1390..1402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1410..1425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1675 AA; 186694 MW; 450E86CCE50EB07E CRC64;
MMAERGWVGS GLQGKKDKFE NFVMAENKSC EQSTIPEDDL GVSEISVYVT NVDGNLPVKR
KQPRKGKMKS KLSRKLRTQS STALYFAGLF RIANVEFVPE YRRKDSPEFL SMAAKIQQVM
NNVYQKSLFS KLYKQSTISD LSNNNGGILV HFWIVFMVPS FKTVFVCEDC VSAVLKDSIQ
TSLVNRTSVG YLLGLPVDMD SIVVNAGLRS DYIATAGTGS EYVMDKSAEQ AGIAVPLNFF
AASGRVSCHF KLTSPPEHVI RLSFSSLKIE PDSCVTDSLA IYDSLMPIRS RNLYRVCEHF
VSFPVSFVST GNGMFLSFKS LRVRGIKEIN GYFEAIPKEK RENTIISTDG ARLEGNISSP
YYPSYYPLKC SRTWTFKMPK PSFGLALTFH NYTVKEKRLE RCDHGWWKIN EKMYCGYQID
HQTVFHIANF LVNIMFQCSG KQSDKAFLAE YSSYNISQPC PNGYYVCSTG LCIRQSQRCD
GSDDCFDESD EVFCSSPSKE CNASSPQHYF LCNGVKDCKN GIDELNCTDS VPCTDITYKC
KNNLCMRKRN AQCDTRVDCL DGSDEMNCDC GNKRQKGSRI VGGSNARDGD WPWQVSLHFS
GSPYCGASVI TKEWLLSAAH CFQGEKLSDP RQWVAHLGMR SQGNAKFTSE LKRILVHEYY
NGRTFDYDIS LLQLKKTWPD TLASAIQPIC VPSLTQVVPN GERCWVTGWG QKQETDNSDP
TVLQQAEVEI INQSLCRSTY GLITPRMLCA GLLSGKRDAC RGDSGGPLSC QERIASRQAL
VGALVEALLI HMLLLPLLWI NMKTMCGKYP QGSALGEVKA MLTFSKQRVS EVFSISEGVA
HHQKEMTATS GQKYPIAGCN KESLPADQCL NLSSAHSVGP LAIKTYLRPL EFSSHRLARS
EPCRRWILGS LPVIPLTAAT IVVILCYCLS PAISIFYLSG SLEISNLTYT NELGDPRSQQ
FISQAQAVQN YFSELYEPSI LGKYYLKSVI TAFSEGEEGL RAYYWSKFSA PENIAHYIKN
ATTSNLQQVN GKKLKVPMLN SSEEISSTEE DFDVYTVELF ASGSEEYDLT VKSAISFDLY
AKPGNNRTLT LTRPKRSYYQ WRLRVPAGHI VHLVILTLHG AIPGNCAIHK LSAYDFLLPV
QNKIITRWCG SPVTWNPPVI RLTSSGNVML VTFSSNVPRG GSVFKAYFEA IRKRDCGGNR
ISWNGSLSSP YYPRYYPPKV DCTWTITTPA VGYIIALSVI VLEIQAGSQG SRNCDKDWLE
IEGIRYCNRI TEGGFSKIYG RSVKIKFHSD QSVTHKGFSL DYKAFSYEDP CPNQFKCKDG
SCISLKNHCD GWRDCLDGSD EIKCNCYFAC PSGNCILHES VCDGINDCGD ESDELNCTRA
AIFPLVHKGC SLSSYKCHNG KCVNKINPEC DGRRDCMDGS DESGCGCGIS PIKKTKIVGG
ENAKKGKWPW QVSLQMGMYG HICGATIVSN RWLVSAGHCF QDSDSIRYST SSAWTAYLGL
RLMNRMNSWI VTRSINRIVT HPKYDEYTSD YDIALLELKT PVFFSDSIQP VCLPATTHVF
STSANCYVTG WGVLGEDGEL ATVLQEASVK IIPLNICNKL YENSVTSRML CAGYLRGGVD
ACQGDSGGPL VCLGKRRKWF LAGIVSWGEG CARRNRPGVY TRVSRFSDWI KQQIN
//
