ID A0A2Y9MBR6_DELLE Unreviewed; 422 AA.
AC A0A2Y9MBR6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=LOW QUALITY PROTEIN: transmembrane protease serine 4 {ECO:0000313|RefSeq:XP_022414858.1};
GN Name=TMPRSS4 {ECO:0000313|RefSeq:XP_022414858.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022414858.1};
RN [1] {ECO:0000313|RefSeq:XP_022414858.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022414858.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR RefSeq; XP_022414858.1; XM_022559150.2.
DR STRING; 9749.A0A2Y9MBR6; -.
DR KEGG; dle:111166903; -.
DR InParanoid; A0A2Y9MBR6; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 2.
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; 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:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 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; 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|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034,
KW ECO:0000313|RefSeq:XP_022414858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|RefSeq:XP_022414858.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..419
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 62..77
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 422 AA; 45996 MW; E4AE19DE678D636D CRC64;
MSPPCANPAP PWRPSEXVGI PIIAALVGLL TIMAVAVLIK VVLDNYFLCG QPLHFIPRGQ
VCDGQQDCAS GEDEQHCVKE FPDGPPVTVR LSRDRSTLQV LDLATKNWAS ACFDNFTEAL
AKTACGQMGY DSKPIFRAVE IGPAQDLDVV KITENMQELQ VRNSSGPCLS GSLVSLQCIA
CGKSLKVPRV VGGEMASVDS WPWQVSIQYD KQHICGGSIL DLHWILTAAH CFWKHLDVSN
WKVMAGSDKL GNFPSLPVAK IFIIQPNITS PKEQDMALVK LQLPLTFSDT VRPICLPFSD
EELPPATPLW IIGWGFTEEN GGKISDILLQ ASVQLIDSSR CNAEDAYQGE VTEKMLCAGI
LEGGVDTCQG DSGGPLMYHS DRWQVVGIVS WGHGCAEPNT PGVYTKTTAY LNWIYNVRKS
DP
//
