ID A0A1L8HMU1_XENLA Unreviewed; 1153 AA.
AC A0A1L8HMU1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Transmembrane protease serine 9 {ECO:0000313|RefSeq:XP_018098995.1};
GN Name=tmprss9.S {ECO:0000313|RefSeq:XP_018098995.1,
GN ECO:0000313|Xenbase:XB-GENE-17336049};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018098995.1};
RN [1] {ECO:0000313|RefSeq:XP_018098995.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018098995.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018098995.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_018098995.1; XM_018243506.2.
DR AlphaFoldDB; A0A1L8HMU1; -.
DR STRING; 8355.A0A1L8HMU1; -.
DR PaxDb; 8355-A0A1L8HMU1; -.
DR GeneID; 108706794; -.
DR KEGG; xla:108706794; -.
DR AGR; Xenbase:XB-GENE-17336049; -.
DR CTD; 108706794; -.
DR Xenbase; XB-GENE-17336049; tmprss9.S.
DR OMA; FWWVIGI; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 108706794; Expressed in internal ear and 9 other cell types or tissues.
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; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 3.
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; 5.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF13; TRANSMEMBRANE SERINE PROTEASE 12; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 3.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 3.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000313|RefSeq:XP_018098995.1};
KW Membrane {ECO:0000313|RefSeq:XP_018098995.1};
KW Protease {ECO:0000313|RefSeq:XP_018098995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000313|RefSeq:XP_018098995.1}.
FT DISULFID 187..199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 207..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 873..885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 893..908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1153 AA; 126058 MW; 1C87A441CB8C72B1 CRC64;
MAEKYADNEP VLDVQKADFL GTPCCRWTVA SLLLGGVTLS ITTALLIMYL TTHSLTMTHT
LEVQGLQYDA SLQNRTSLYH RSLTNTLQRL LRSSFRNTVA EEIYVECAIL QYRQGNESII
AYLKLQFLAS GHFPGNEEIE KLLRQGLALF LRGNTIPVPT FGNISSAVLT DNHGLSFNSI
DLKSGSCPAH IFACKNTQCI VKQNPECDNI RDCKDGSDEK NCNCGTRPAM QKTNRIVGGS
DATKGEFPWQ VSLRESNEHF CGATVIGDKW LVSAAHCFND FQDPAVWVAF IATTSLSGTD
SSTVKSTIKN IIKHPSYDPD TADYDVAVLE LDSPLKFNKY TQPVCLPDPT HVFPVGKKCI
ITGWGYLKED NLVKPEVLQK ATVAIMDQSL CNSLYSNVVT ERMLCAGYLE GKIDSCQGDS
GGPLVCEEPS GKFFLAGIVS WGVGCAEARR PGVYVRVSKI RNWIMNIISS FVALDSQTSL
TTTTTTTTTT GGKKTTNAKS TTARPFTKHS TTRAKPAIST LPSKPTQKPF STIKPQECGS
RPGLTKPNKI VGGLDAVRGE IPWQASLKEG SRHFCGATII GDRWLVSAAH CFNQTKVDQV
TAHMGSTSLS GADTIAVKIS LKRVIQHPHF NPLTLDFDVA VLELANSLTF NKYVQPVCLP
SALQKFPAGW KCMISGWGNI KEGNVSKPEI LQKASVGIID QKICSVLYNF SITERMICAG
FLDGKVDSCQ GDSGGPLACE ESPGIFFLAG IVSWGIGCAQ AKKPGVYSRV TKLKDWILDT
VAPVLRTTDS GMNLPRSSSL PITATRLSTF QPATSTGRRT TLSRHTMSQT KSTRSTPKST
TKYTSKKTTI AKTSPTALRI TEPVRATQRP VPCSASTYKC SNRVCISKPN PECDGIQDCN
NGSDEQNCDC GFAPVLPYNK IVGGSGSVRG EWPWQVSLWL RRKEHKCGAV LISDRWLLSA
AHCFDIYSDP KLWAAYLGTP FLNGVEGRVE KIFRIHKHPF YNVYTLDNDV ALLELPSPVT
YTNLIRPICL PDISHIFPEG TRCFITGWGS TKEGGAMSRQ LQKASVSIVG DQTCKKFYPI
QISPRMMCAG FMQGGVDSCS GDAGGPLACR EPSGRWFLAG ITSWGYGCAR PYFPGVYTRI
TSIRNWIGQN LRL
//