ID A0A091DMP9_FUKDA Unreviewed; 699 AA.
AC A0A091DMP9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE RecName: Full=FXYD domain-containing ion transport regulator 3 {ECO:0000256|ARBA:ARBA00069737};
DE EC=3.4.21.106 {ECO:0000256|ARBA:ARBA00066639};
DE AltName: Full=Serine protease hepsin {ECO:0000256|ARBA:ARBA00068145};
DE AltName: Full=Sodium/potassium-transporting ATPase subunit FXYD3 {ECO:0000256|ARBA:ARBA00077038};
GN ORFNames=H920_06217 {ECO:0000313|EMBL:KFO32372.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32372.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO32372.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO32372.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with and regulates the activity of the
CC sodium/potassium-transporting ATPase (NKA) which transports Na(+) out
CC of the cell and K(+) into the cell. Reduces glutathionylation of the
CC NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated
CC inhibition of ATP1B1. Induces a hyperpolarization-activated chloride
CC current when expressed in Xenopus oocytes.
CC {ECO:0000256|ARBA:ARBA00059844}.
CC -!- FUNCTION: Serine protease that cleaves extracellular substrates, and
CC contributes to the proteolytic processing of growth factors, such as
CC HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell
CC morphology. Plays a role in the proteolytic processing of ACE2.
CC Mediates the proteolytic cleavage of urinary UMOD that is required for
CC UMOD polymerization. {ECO:0000256|ARBA:ARBA00058223}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage after basic amino-acid residues, with Arg strongly
CC preferred to Lys.; EC=3.4.21.106;
CC Evidence={ECO:0000256|ARBA:ARBA00051268};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004655}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004655}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the FXYD family.
CC {ECO:0000256|ARBA:ARBA00005948}.
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DR EMBL; KN122176; KFO32372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DMP9; -.
DR STRING; 885580.ENSFDAP00000007905; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProtKB-ARBA.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043269; P:regulation of monoatomic ion transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR CDD; cd20328; FXYD3-like; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 1.20.5.780:FF:000006; FXYD domain-containing ion transport regulator; 1.
DR FunFam; 3.10.250.10:FF:000020; serine protease hepsin; 1.
DR FunFam; 2.40.10.10:FF:000003; Transmembrane serine protease 3; 1.
DR Gene3D; 1.20.5.780; Single helix bin; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR047297; FXYD_motif.
DR InterPro; IPR015352; Hepsin-SRCR_dom.
DR InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
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:SF7; HYALIN; 1.
DR Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
DR Pfam; PF09272; Hepsin-SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01310; FXYD; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glutathionylation {ECO:0000256|ARBA:ARBA00023206};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Sodium/potassium transport {ECO:0000256|ARBA:ARBA00022607};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 648..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 189..431
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 677..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 75632 MW; D655461CDD1AF6A9 CRC64;
MVSVAGGRIV PCSRPKVAAL TVGTLLLLTG IGAASWAIGE SGWPLCLYPP QPVPPASCLT
SAFSVVTVLF RSDQEPLYPV QVSPVDARLM VFDKTEETWR LLCSSRSNAR VAGLSCEEMG
FLRAVAHSEL DVWTAGTNGT SGFYCVDEGR LPQARRLLEV ISVCDCPRGR FLATVCQDCG
RRKLPVDRIV GGQDTSLGRW PWQVSLRYDG AHLCGGSLLS GDWVLTAAHC FPERNRILSR
WRVFAGAVAQ ASPQGMQLGV QAVVYHGGYL PFRDPTSEEN SNDIALVHLS NPLPLTEYIQ
PVCLPAAGQA LVDGKICTVT GWGNTQYYGQ QAAVLQEARV PIISNNVCNS PDFYGNQIKP
KMFCAGYPEG GVDACQGDSG GPFVCEDSIS RTSRWRLCGI VSWGTGCALA QKPGVYTKVS
DFREWIFQAI KWPPGGSFTV PGSRIFSILS VADTSSVTSR VPRLSLDIFA VLNGCAYHGG
SDRILRVALQ AHGALCQDAN VTAGHWRSPS FGVTCGLHLE KCRPEKKCRP AFTGVGKVLA
YNSDEKYQER LMHYQERQET FPGVHQIYLV TAAPSGLTLF LLHRILNSCL ASLAAHKQNL
LRHSATGHCS DMQEVALSLL GLLAGLPALD ANDPEDKNSP FYYDWHRLRV GGLICAAILC
ALGFIVLLSG KCKCKFSQKP SHHGPDAPPL ITPGSAHNC
//
