ID A8X925_CAEBR Unreviewed; 2592 AA.
AC A8X925;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 28-JAN-2026, entry version 124.
DE SubName: Full=Protein CBR-FMI-1 {ECO:0000313|EMBL:CAP29137.1};
GN Name=fmi-1 {ECO:0000313|WormBase:CBG09454};
GN Synonyms=Cbr-fmi-1 {ECO:0000313|EMBL:CAP29137.1};
GN ORFNames=CBG09454 {ECO:0000313|WormBase:CBG09454}, CBG_09454
GN {ECO:0000313|EMBL:CAP29137.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29137.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP29137.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29137.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000313|EMBL:CAP29137.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29137.1,
RC ECO:0000313|Proteomes:UP000008549};
RA Ross J.A., Koboldt D.C., Staisch J.E., Chamberlin H.M., Gupta B.P.,
RA Miller R.D., Baird S.E., Haag E.S.;
RT "Caenorhabditis briggsae recombinant inbred line genotypes reveal inter-
RT strain incompatibility and the evolution of recombination.";
RL PLoS Genet. 7:E1002174-E1002174(2011).
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}.
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DR EMBL; HE600954; CAP29137.1; -; Genomic_DNA.
DR RefSeq; XP_002636973.1; XM_002636927.1.
DR FunCoup; A8X925; 656.
DR STRING; 6238.A8X925; -.
DR GeneID; 8578968; -.
DR KEGG; cbr:CBG_09454; -.
DR CTD; 8578968; -.
DR WormBase; CBG09454; CBP47604; WBGene00031032; Cbr-fmi-1.
DR eggNOG; KOG4289; Eukaryota.
DR HOGENOM; CLU_231552_0_0_1; -.
DR InParanoid; A8X925; -.
DR OMA; DAYYTYT; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0033564; P:anterior/posterior axon guidance; IEA:EnsemblMetazoa.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097376; P:interneuron axon guidance; IEA:EnsemblMetazoa.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR FunFam; 2.60.40.60:FF:000104; cadherin-23 isoform X1; 1.
DR FunFam; 2.60.40.60:FF:000135; cadherin-23 isoform X1; 1.
DR FunFam; 2.60.40.60:FF:000020; Dachsous cadherin-related 1b; 1.
DR FunFam; 2.60.40.60:FF:000080; FAT atypical cadherin 1; 1.
DR FunFam; 1.20.1070.10:FF:000456; FlaMIngo (Cadherin plus 7TM domain) homolog; 1.
DR FunFam; 2.10.25.10:FF:000949; FlaMIngo (Cadherin plus 7TM domain) homolog; 1.
DR FunFam; 2.60.40.60:FF:000324; FlaMIngo (Cadherin plus 7TM domain) homolog; 1.
DR FunFam; 2.60.40.60:FF:000362; FlaMIngo (Cadherin plus 7TM domain) homolog; 1.
DR FunFam; 2.60.40.60:FF:000421; Protein CBG29115; 1.
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; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR056286; Cadherin_CELSR1-3_9th.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR055928; Fmi-1_DUF7505.
DR InterPro; IPR057244; GAIN_B.
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; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR PANTHER; PTHR24026:SF51; PROTOCADHERIN-LIKE WING POLARITY PROTEIN STAN; 1.
DR Pfam; PF00028; Cadherin; 7.
DR Pfam; PF23592; Cadherin_CELSR2_9th; 1.
DR Pfam; PF24337; DUF7505; 1.
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; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50221; GAIN_B; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002730242"
FT TRANSMEM 2225..2246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2258..2278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2290..2310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2322..2343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2355..2379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2399..2419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2431..2450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..270
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 271..375
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 375..478
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 479..580
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 581..681
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 682..799
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 800..907
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 908..1015
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1266..1302
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1348..1541
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1592..1747
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1772..1804
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1891..1966
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2050..2215
FT /note="GAIN-B"
FT /evidence="ECO:0000259|PROSITE:PS50221"
FT REGION 2485..2526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2511..2526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1292..1301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1794..1803
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2592 AA; 288219 MW; ECDCA66A6DD0E587 CRC64;
MMLNKIMFLP FFITSSLLLV SALTEDKYYS SEPISVVCKP CAVPSSSFVI WLPASRPPCL
HPGQPIIHWP DSSSSDITSC PIPGFPDSIQ SSQLSLLDDG LLLTKERVCF FDGPIDFHYN
YVCDGQIYQS KMRIGHSVAS MKKLEIRRTK RWARRRNPDA NAVHFQQEKY VKELPEDTPI
ETVIASVKAS HASSQPLYYS MVAPQDSRSQ NLFTLDTMSG EIRLAKSMDR EVLDKHILKV
TAYERVDPTI SASTTVVVHV LDVQDNSPIF EKDSYFGEIR EDAPIGTTVL SVFARDLDSE
ENGEVEYSLG EGNGKNLLAI NSKSGVIQTA APLDRETLSL IRLDVIASDK GIPKKESKAL
VEITVLDVND NAPVFASDSY ITILENITLP TVIATVKATD EDFGTNGKVH YSMASSSGIG
GLTIDYSSGE VTLRERIDAK NSPITAIIRA KDGAQPALSS TVSLTIHVVD INDHAPTLIA
AQKMITLEEN VAIGEEVGRV YAIDEDSGPN GIIRYSIEGS EDFIIDEDSG VIKTTKLLDR
ETTARYSLKV TARDMGTPPL NTSTTMTVVL KDINDNAPIF DKKEYNVTIS EEMPRGSQII
KWKAVDNDED QKITYRIEEA DRDVFSILDI GDQGAILSVS GQLNKQDHKI RVEVSATDQG
GLQGRCVVNV FIDDVNSAPY FNDHPFSVKI PEHSPIGYPV ISMKVCDFAN GFRFISKLFP
AEDHDRGDNA RLVYSIDSNQ FFKIDPSSGD ISVASDLDRE DRATFSVIVT ASDHATPPLN
TSTQIEVILD DINDNAPQFT SSSYAATISE DIPVGTSFLQ VSAIDADIGS NGIVDYFLNE
SSSSPAIHLF RLDRTSGTLR VSSKLDREQF AVILLPIFAR DRGTPSLSAS SEITLTLSDV
NDNAPSFEQL SYDLYIAENA PAGSTVGTIV ARDADEGENS DISFRIFGGT DAKLFDIEED
AEQNGVVRIL TRAEFDYEAK SNKFFFELQA SSGQLSSTVP VRIHVSDVND NKPVLKDFVI
LMNRFDNVQM AKQIGFIPSF DPDQNATLEY FLEENDLIEA EKYTGKILVK QEWKRNMDVS
FKTCVSDGAN TECATCRFIH VLVEPDWLAE SFTLSLARMT VDDFWDPLVF QRFRDAMSTL
SNWKPSDIHV IGVKQHLDDV IYINLAITDH GRVVRGWRAI ELVKESIKKL EKMTLLQVEV
IRDESCANEP CSHMAKCRQT QKFVGEMKAH ETDNFIARTL NTVNTFVCEC PSGFTSSDGR
GECDTRLDEC YRGRCSNNST CVAYENTYRC ECKPGWIGRH CEISVHALTC VPGYCMSDSL
CELEGNRMRC RHCKYQGEDT DERCRLRSVS FEGEGILNVN LDLPRTQWTM KFRISTIAHD
GVLVFTGDKR SDFVEVSIVD RVLKVQFSLG GEKADAKMEN DVENRVNDGE WHTVTVEFSN
KQITMSLDDC ETHPSLLLNS SPNCAVRAKL NLEKKCEDPT VPCYRYMDVS NGLFLGGRPG
TSKQIEKAFS GCISDLSVDK EDVDFSTIKE MHKVGHVHEG CRQRRDFCSS SDGQCSATTK
CSNRWGGRIC SCPQAVHSLG ECIVPVGNQD LRGHSLFEEE SFVLYQPAQV SVPFEVSFEF
RSSRADMQVF ALEFTQRSVH YNLEIDDGTL KYNIGDSSVE LPSPEITSKH WMNVVVKFEA
DSVATSINGI YSAEAKTSIA DMNLESLYYG IAPGTGHPSR FEGCIRNVMV DGRPVSVKKK
GKTRAGCVVP NRCSVDSICP SDRDTCLPVC SVANVCSSGT CVASNTTTGY ECICPPGRTG
KNCQLEAPKQ ICPSGWWGTF PRCRRCACSQ SKGYESQCDK KTGACLCKKS HFSTINGCVK
CECGSGSEST ECSSDGYCKC NGDSVGRRCD RCSRYDHQLD SKTLKCRPVA GKCPSEIEYS
IQWPISQKGS IVRQSCPIGE SGLATRKCLE TGRWSDVNAW NCTRPEYSIM VNKFDILEPA
KLLTMVSNAT NTESSIRGRN QQIAAEALSR LVDHEQMIPL KGRAHIKDMT FTERLIEALG
RVMSEQPADE YSTMIAKLWS YAETVAETHE SVSFLSPFFV TNDHIVFASD KLDFGNMLPK
FNNFVDLRPT GFPRVRAIVT GTTQVVYSIV PYPRCDRCEN PMIAVVANTT DPIIVEFEID
EDDGWKYPEC VRFDDQSGAW TNRGASLIGL NLTHAACEYD RIGVFTMFVN DHSNSIVRVA
QIDDMTSPAI AGVALFLCFL SILLTISRKS LKTHSVRIGF ILFFAINVLN LFFVHKTAIN
QAFCPVRNAM LSFTSSSPFA WLFLYGLYIY RMLADGSSSP SVATSLLVGI VFPCIISFTT
FFFTDTCSLS PHLWLFWFIV LPIGLFLLLS FYAASTSVLV SLHKKYDVFV AKYNVKKAVF
QHFVLTLFTL VMTLSGLFAN QLPLPMEIVE ISQSVIYLIA SIVIFLWCIC DMTSKSTDSN
PNMWLDTQKS VMAESTMADP QCASPLLSPQ NHHHDAGVDP DWMPDVIPNN HHLSSINEPD
TPRRQLQPQN REVINILSSP DKILNEGIGH VYRNNMGSLP RLRSEQDEAD DAYYTYTASR
RYKNTTSTFN RE
//
