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Database: UniProt
Entry: A0A060XB30_ONCMY
LinkDB: A0A060XB30_ONCMY
Original site: A0A060XB30_ONCMY 
ID   A0A060XB30_ONCMY        Unreviewed;       988 AA.
AC   A0A060XB30;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=SRCR domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSONMT00024835001 {ECO:0000313|EMBL:CDQ76437.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ76437.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ76437.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ76437.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; FR905141; CDQ76437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060XB30; -.
DR   STRING; 8022.A0A060XB30; -.
DR   PaxDb; 8022-A0A060XB30; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001190; SRCR.
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; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF11; TRANSMEMBRANE SERINE PROTEASE 2; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50287; SRCR_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};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
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|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
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};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT   TRANSMEM        81..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          627..675
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          739..984
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          199..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  110935 MW;  7B11D67B371E62CA CRC64;
     MFGPEITVSV SLCGLQGQTW QCSVCCVPSG SRPRRLCSST WRFMQGCTAT SAATVTTPSP
     ATPPSNATCG HTQVRTASVS IVIFIIPIII TTTVFIIIII TVTTRLSVTM FSTVISNSCA
     LYGDYGNYGP PPYPRKNIRP RASLRHNPYN PYRPYLRRVD TRVSLANPNK ISRTTSRGQY
     VTMPVHHPKL HPLPVSQRII QSQHKARQTK SAERFSSYDT SSWIEKGSSK PNRGKKTQNK
     ATSSSSKSTG DIRHKSSSSN VRQHHRYFTK DGMCRGSSYS SKNKMCDLIG TLVDLKYSWI
     LFVFTLCYIV TWAAFAELYF LGAWLRGDME HIQDPQWQPC FEKLNSFHSA LSISMDSQII
     NGYGSRVASA NCMDGLVLMM AQSIIESVLD TLMLGCILAK LARPKRRLPT LLFSQHCVVS
     ERDERLCLMF NVKTLKETHM LVAEIRAKLI KSHHTKEGEF ILLEQRELTL GMGPDGARLF
     TVEPQTVEHV IDEQSPLWGI SADSLEWDTF EIVVMVDGAV QDAGTAFHVR TSYTEDEIFW
     GQRFKSHKPL EKRGIGSNHK TSDKNYKVQT ATHSDREMAV RQRHERSPGH DTDSVPSNMP
     TRKVHYQYLS DQMLLCNSVT NNIGTGTRKL SSVFYRISPE NSLLEIQLEK VPTWLPVCYE
     RWNSSLGTLV CRQLGYLRLQ KGVNLTDIGP NYTDGFIQIT SEHNSSLENI WQLRGSCVTG
     KVIALKCFEC GTRAKLPRII GGVEATLGRW PWQVSLYYSN RHTCGGTIIT SQWVVTAAHC
     VHNYRLPQVS SWVVYAGIVT RSSAKMSQYI GYPVEKILYN KNYNPRSHDN DIALMKLRTP
     LNFSGDRELD CFYTIRPICL PQYERDLPGG TQCWISGWGY TQPDDVLIPA TLKEAPVPLI
     STKKCNSSCM YNGEITPRML CAGFTEGKVD ACQGDSGGPL VCQIDNVWRL VGVVSWGTGC
     AEPNHPGVYT KVAEFLGWIY DMIEANLH
//
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