ID A0A087V7H5_BALRE Unreviewed; 701 AA.
AC A0A087V7H5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Transmembrane protease serine 7 {ECO:0000313|EMBL:KFO08567.1};
GN ORFNames=N312_08615 {ECO:0000313|EMBL:KFO08567.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO08567.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO08567.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO08567.1};
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; KL482901; KFO08567.1; -; Genomic_DNA.
DR RefSeq; XP_010296049.1; XM_010297747.1.
DR AlphaFoldDB; A0A087V7H5; -.
DR GeneID; 104632010; -.
DR KEGG; breg:104632010; -.
DR CTD; 344805; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000053309; 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; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
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; IPR001314; Peptidase_S1A.
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; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
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; 3.
DR PROSITE; PS50024; SEA; 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}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000313|EMBL:KFO08567.1};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:KFO08567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000313|EMBL:KFO08567.1}.
FT DOMAIN 1..91
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 100..217
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 222..335
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 464..698
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 341..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 348..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 360..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 395..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 416..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 436..451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 701 AA; 77650 MW; A07751BF336F1854 CRC64;
MNLVYTASSF SKFYKQSTVS EVSNNNNGGL LIHFWIVFVV PQAKGQVLCE DCVAAILKDS
IQTSIINRTS VGSLQGLAVD MDSIVLSAGL RSDYWSTTGT GANCMYDLYA DRLHEHFPLD
IHATSGGTIC YFKLIASVGH LIRLSIESLQ IEADNCITDS LTIYDSLMPI KHKILYRACE
PVDSLVSLVS TNNLMLVTFK AAQIKERKEF HGYFEVITQE RCGKAIVTKE KIGYEGRITS
PYYPSYYPPK CLCAWNFQTP QKSLGIALKF HNYTISEKNI KGCERGWWKI NEHTYCGYYV
DHQTVFHIAS SAVNIELQCS SKVSEKPLLV EYSSYNISQP CPPGHFKCST GLCIQQMQRC
DGINNCSDES DELSCAVPEW NCNSSFAIQD NLLACNGVSD CEDGKDEQNC THSIPCTNRT
FKCKNNICIR KQNAKCDGIV DCVDGSDESS CSCGSSSSNP ISRIVGGANT EEGEWPWQVS
LHFVGAAYCG ASVISNEWLV SAAHCFQGSK LADPRAWRAH LGMRMQGRAK FVSAVRRIVV
HEYYNSGNYD YDIALLQLSK PWPDTMSHVI QPICVPPFSH KVRSGDKCWI TGWGQKQETG
DEGSVILQKA EVEIIDQTIC RSTYGIITAR MFCAGLMSGK RDGCKGDSGG PLSCQSNGDG
KWFLTGIVSW GYGCGRPNFP GVYTRVSNFA PWIHKYVPSV L
//
