ID A0A0V0URK1_9BILA Unreviewed; 1217 AA.
AC A0A0V0URK1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=JNK1/MAPK8-associated membrane protein {ECO:0000313|EMBL:KRX53681.1};
DE Flags: Fragment;
GN ORFNames=T09_8179 {ECO:0000313|EMBL:KRX53681.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53681.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53681.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53681.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX53681.1}.
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DR EMBL; JYDN01000194; KRX53681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0URK1; -.
DR STRING; 181606.A0A0V0URK1; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140042; P:lipid droplet formation; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:InterPro.
DR CDD; cd12446; RRM_RBM25; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.20.1390.10; PWI domain; 1.
DR InterPro; IPR008485; JAMP.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034268; RBM25_RRM.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR18806; RBM25 PROTEIN; 1.
DR PANTHER; PTHR18806:SF4; RNA-BINDING PROTEIN 25; 1.
DR Pfam; PF05571; JAMP; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF06775; Seipin; 1.
DR SMART; SM00311; PWI; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF101233; PWI domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 847..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 995..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1096..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1161..1179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1185..1205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..166
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 623..722
FT /note="PWI"
FT /evidence="ECO:0000259|PROSITE:PS51025"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX53681.1"
SQ SEQUENCE 1217 AA; 140493 MW; A220FBBBA6920182 CRC64;
LKLYEEMAFP PRFGMPSIAQ ATFVPTYNAV PVVLPTTAHY LMPTLANSGV VRNVVQKTPS
PAPLTKRQEI LMEKPPVTTV FVGNINEQAT NEMIKAMLVK CGNIISWKRI QGPNGKFQAF
GFCEYDHPDS TLRALRLLHD WPLGDKKLVL KCDEKNKSML IDFINKRRSL YNKPPLKMEG
DQLPADDEIR KEDEMFRKAL KSLVKEMAPE LFEGTSKSHV PKSPTLTGKG GNLDIESLDR
DRKEYIAKEI IQFREAHKDD KEARLKGKSA SVDVNEKNER FTERSSSPLE ADRRASTKFE
RSCATDSADA KAGEARGRRR GSTPETGSRR RRSPSADRLL ETSEDARERE KLERKAREKE
KNYLERLEKL EAREKRKAKE RLKQAEKEKR RKKEQLADIK IMQEFLEDYI DEEGDLEFYQ
GKSLLLRKDA ITDEMEWDAL DRLREAEEIA LIRRKLIEEN SSKDSNETKI MVEELPVNPV
KLEEQQRTVS ESETDKAADN NDNNADEVDS AVPKVKKETV LIPTVFLPAQ AENSQPIGFA
GLKLGSVSTS TNTAAPIPLQ QMFNEPDEEF SVVKTSSRKL VPLEYTEEEK RALEMPNMHT
QMSTEERKKY VKSLIDKIPS SKEELFKYEI HWEYVDQLLI DRRIKPWISK KIIEYIGEEE
ASLVDFISEK VLERSTPQGL LDDISMVLDE EAGVFVAKLW RLLIYEIEAK RVDFYYDVLF
ELTVFPDSVR PTSGMIMLIV RCYSGENLLT YSFPRSTILI YRPWPWRLIR MFVKLPLYVF
GCCNEEQTFS INLLEKFHFS SAHFCSKISV ELQNTEMNIV RSSIILQPCV NLLFHFFFRW
PFSSIPLLYM FLCALFTAIS LFLWIYLIAV KVTEIQHPTY KENIVMDNFL FDNPEPCPGL
YCGRQVISDG NYTECGVSIL FFHIFHLVLE ANRIYLLACD WGTRVNERGI CVPCNGYPDV
YDWLYLGFMG FLPFLLHCAS IKFTSAHTRE FRNVVLPQIA AAFVECVFPA ILSLLIVEPK
GSLNFYTCGV QNLQDWYPVF YNPVIDYTRT VHCTQEAVYP LYFLPFVYYL FSLLSLSIIH
PIVVCVFKLK KEGASGAIYA ALYFYPILII LHSVLCGLIY YAFPYIILFA AICLNAMHLA
LYETQTPICI LHDMWRKKQN LAVLGVLIYL YLYGILSISR FSSYWVYNVM LLFIPAPSIF
YVLTVKFTHP HRLNMII
//
