ID A0A2G5TJ33_9PELO Unreviewed; 2465 AA.
AC A0A2G5TJ33;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC27300.1};
GN Name=Cni-fmi-1 {ECO:0000313|EMBL:PIC27300.1};
GN Synonyms=Cnig_chr_V.g19604 {ECO:0000313|EMBL:PIC27300.1};
GN ORFNames=B9Z55_019604 {ECO:0000313|EMBL:PIC27300.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC27300.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:PIC27300.1}.
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DR EMBL; PDUG01000005; PIC27300.1; -; Genomic_DNA.
DR Proteomes; UP000230233; Chromosome v.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 8.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF445; CADHERIN-87A; 1.
DR Pfam; PF00028; Cadherin; 7.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2098..2119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2131..2151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2163..2183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2195..2216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2228..2255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2276..2295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2307..2326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..139
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 140..244
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 245..348
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 349..450
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 451..551
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 552..653
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 654..761
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 762..869
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1120..1156
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1202..1395
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1446..1601
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1603..1640
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1645..1677
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1764..1839
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT REGION 2382..2401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2383..2401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1146..1155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1630..1639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1667..1676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2465 AA; 273961 MW; F24E55478B3114A9 CRC64;
MRIGHSIASM KKLEIRRTKR WARRRNPDAN AVHFQQEKYV KELPEDTPLE TVIASVKASH
ASSQPLYYSM VAPQDSRSQN LFTLDTMSGE IRLAKSMDRE VLDKHILKVT AYERVDPTIS
ASTTVVVHVL DVQDNSPIFE KDSYFGEIRE DAPIGTTVLS VFARDLDSGE NGEVEYSLGE
GNGKNLLAIN SKSGVIQTAA PLDRETLSLI RLDVIASDKG IPKKESKALV EITVLDVNDN
APVFASDSYN ITILENITLP TVIATVKATD EDFGTNGKVH YSMASSSGIG GLTIDYSSGE
VTLRERIDAK NSPITAIIRA KDGAQPALSS TVPLTIHVVD INDHAPTLIA AQKMITLEEN
VAIGEEVGRV YAIDEDSGPN GIIRYSIEGP EDFIIDEDSG VIKTTKLLDR ETTARYSLKV
TARDMGTPPL NTSTTMTVVL KDINDNAPIF DKKEYNVTIS EEMPRGSQII KLKAVDNDED
QKITYRIEEA DRDVFSILDI GDQGAILSVS GQLNKQDHKI RVEVSATDQG GLQGRCVVNV
FIDDVNSAPY FNDHPFSAKI PEHSPIGYPV ISMKAEDHDR GDNARLIYSI DSNQFFKIDP
SSGDISVASD LDREDRATFS VIVTASDHAT PPLNTSTQIE VILDDINDNA PQFTSSSYAA
TISEDIPVGT SFLQVSAIDA DIGSNGIVDY FLNESSSSPA IQLFRLDRTS GTLRVSSKLD
REQFAVIVLP IFARDRGTPS LSASSEITLT LSDVNDNAPS FEQLSYDLYI AENAPAGSTV
GTIVARDADE GENSDISFRI FGGTDAKLFD IEEDAEQNGV VRILTRAEFD YEAKSNKFFF
ELQASSGQLS STVPVRIHVS DVNDNKPVLK DFVILMNRFD NVQMARQIGF IPAFDPDQNA
TLEYFLEEND LIEAEKYTGK ILVKQEWKRN MDVSFKTCVS DGANTECATC RFIHVLVEPD
WLAESFTLSL ARMTVDDFWD PLVFQRFRDA MSTLSNWKPS DIHVIGVKQH LDDVIYINLA
ITDHGRVVRG WRAIELVKES IKKLEKMTLL QVEVIRDESC ANEPCSHMAK CRQTQKFVGE
MKAHETDNFI ARTLNTVNTF VCECPSGFTS SDGRGECDTR LDECYRGRCS NNSTCVAYEN
TYRCECKPGW IGRHCEISVH ALTCVPGYCM SDSLCELEGN RMRCRHCKYQ GEDTDERCRL
RSVSFEGEGI LNVNLDLPRT QWTMKFRIST IAHDGVLVFT GDKRSDFVEV SIVDRVLKVQ
FSLGGEKADA KMENDVENRV NDGEWHTVTV EFSNKQITMS LDDCETHPSL LLNSSPNCAV
RAKLNLEKKC EDPTVPCYRY MDVSNGLFLG GRPGTSKQIE KAFSGCISDL SVDKEDVDFS
TIKEMHKVGH VHEGCRQRRD FCSSSDGQCS ATTKCSNRWG GRICSCPQAV HSLGECTVPV
GNQDLRGHSL FEEESFVLYQ PAQVSVPFEV SFEFRSSRAD MQVFALEFTQ RSVHYNLEID
DGTLKFNIGD SSVELPSPEI TSKHWMNVVV KFEADSVATS INGIYSAEAK TSIADMNLES
LYFGIAPGTG HPSRFEGCIR NVMVDGRPVS VKKKGKTRAG CVVPNRCSVD SICPSDSTCH
RAWNKHKCKC QKSFVGDTCL PVCSVANVCS SGTCVASNTT TGYECICPLG RTGKNCQLEA
PKQICPSGWW GTFPRCRRCA CSQSKGYESQ CDKKTGACLC KKSHFSTING CVKCECGFGS
ESTECSSDGY CKCNGDAVGR RCDRCSRYDH QLDSKTLKCR PVAGKCPSEI EYSIQWPISQ
KGSIVRQSCP TGESGLATRK CLETGRWSDV NAWNCTRPEY SIMVNKFDIL EPAKLLTMVS
NATNTESSIR GRNQQIAAEA LSRLVDHEQM IPLKGRAHIK DMKFTERLIE ALGRVMSEQP
ADEYSTMIAK LWSYAETIAE THESVTFLSP FFIANDHIVF ASDKLDFGNV LPKFNNFVDL
RPTGFPRVRT IVTGTTQVVY SIVPYPRCNR CENPMIAVVA NTTDPIIVEF EIDEDDGWKY
PECVRFDDKS GVWTTRGASL IGLNLTHAAC EYDRIGVFTM FVNDHSNSIV RVAQIDDMTS
PAIAGVALFL CFLSILLTIS RKSLKTHSVR IGFILFFAIN VLNLFFVHKT AINQAFCPVR
NAMLSFTSSS PFAWLFLYGL YIYRMLADGS SSPSVATSLL VGIVFPCIIS FTTFFFTDTC
SLSPNLWLFW FIVLPIGLFL LLSFYAAATS VLVSLHKKYD VFVAKYNVKK AVFQHFVLTL
FTLVMTLSGL FANQLPLPVE IVEISQSVIY LIASIVIFLW CICDITSKST DSNPNMWLDT
QKSVMAESTM ADPQCASPLL SPRNHHHDAA VDPDWMPDVI PNNHHLSSIN EPDTPRRQLQ
PQNREVINIL SSPDKILNEG IGHVYRNNMG SLPRLRSDQD EADDAYYTYT ASRRYKNTTS
TFNRE
//
