ID A0A2G5SLY7_9PELO Unreviewed; 1728 AA.
AC A0A2G5SLY7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC16038.1};
GN Name=Cni-crb-1 {ECO:0000313|EMBL:PIC16038.1};
GN Synonyms=Cnig_chr_X.g22786 {ECO:0000313|EMBL:PIC16038.1};
GN ORFNames=B9Z55_022786 {ECO:0000313|EMBL:PIC16038.1};
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:PIC16038.1, 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 -!- 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:PIC16038.1}.
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DR EMBL; PDUG01000006; PIC16038.1; -; Genomic_DNA.
DR STRING; 1611254.A0A2G5SLY7; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 8.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 21.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00008; EGF; 7.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00181; EGF; 26.
DR SMART; SM00179; EGF_CA; 19.
DR SMART; SM00274; FOLN; 4.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 18.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS00022; EGF_1; 23.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 22.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013828496"
FT TRANSMEM 1665..1691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..56
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 136..172
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 174..210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 213..250
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 293..330
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 331..369
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 376..413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 414..450
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 564..723
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 725..761
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 767..958
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 954..989
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1180..1217
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1219..1255
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1257..1293
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1296..1333
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1336..1371
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1373..1409
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1411..1448
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1449..1485
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1487..1523
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1525..1562
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1564..1600
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1615..1654
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 27..44
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 46..55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 162..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 200..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 240..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 320..329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 359..368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 403..412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 440..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 751..760
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 958..968
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 979..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1207..1216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1245..1254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1283..1292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1323..1332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1340..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1361..1370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1399..1408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1438..1447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1453..1463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1475..1484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1513..1522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1590..1599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1644..1653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1728 AA; 189514 MW; F2E41F83D916518D CRC64;
MKYLHFLIFC TLVTNGLSDR ACSRNTCLNG GTCTVNDETR MFQCECPQGF SGLLCQDNCG
LHCLHGNCLK GTFGEETCQC SEGWMGSLCD ILVTDDDSAT AQKCSPQCGD DERCTKGADG
LYFCQNTTVK NTTTTLLSSC ATHTCQNNGT CLADNGDVKC SCQPGFSGEH CEIDEDECQE
HFCQNEAECE NLIGSYKCNC LSGFSGRYCE VQDKKQCTQD FCMNNGQCVL SSSSELSCKC
QDGFQGDRCE QKVNDPLISC TCDNPAHVCS IVNGSTQCEC PSGFMGADCK ELKARPCDIG
PCLNGGHCVD DGQNLFTCFC LPHWTGVYCG EPVECLVNGK DCRNGGKCVF LLTSTSCECP
EGFTGSNCEV SNSYRSHPTC SDIRCQNGGA CKLDAEGEPY CDCPEGFDAP FCEPKSGCTI
NPCQNGGTCQ DADGQYFCHC TSGFGGVHCE TLEEPSTPIP TLGTFPSFTT SGIDQSNLAE
ITCEDCVNSM NCLETESGAV CVCQEEYFGQ KCDQKHNKCA KITCPVGQSC SQISENSNIT
AQCGCEIGHS GLKCDMVTSA TFTAKSLYIH QSSKFSLGTS SFENVAYELE FSFRTTVENT
HLASSENILG EKILSIQLLS GYLVFNVTGN FMTHLLPMRI NDAHWYTVSV KGDNDKIEIQ
VLNENGFKLV KKELSGQLEV FLTRFGKVSG AHHFIGCMAD VRVDGELIIF TDSKRAIEIR
KGCTRSEQCS RAYCQNDGVC VDHWESSSCK CKSPFLKPNC AYFLPKTTFG HLDQPSIVHL
STSETENHLL RTQIELSFLM RSGKPDAVLF YIGEKHAADV LTNYLVVKIA SGFVSVRYRT
GGRREVEFTS KNHVDDNEEH HVQISVDKNR RQIIIDDLTE CSEPIISRMS QEFYVDDILI
GASNAVATDS EFYKGYLQDI QLNQKSVVIH PTSLTIEKIG KLEKTQNVIE GAVSDPMCNS
NVCKHGECSE TFNDYTCQCS DGSTGRHCDK IDYCREAKCM EGSKCENAEN GHFCVFTITI
SNGSKLTYSI EPKSILSVPS VKFSIRSHSS NGHIFTLNIG KSTVSAMIFK RRLVLVSNPQ
NQKFDTVIAD GKWHNITLHP FKVIIDEKSY ISTTQLFPSE SKTEASLFIG EQGQDVIFAC
LDDFQLGNYP KLSFTKAKIP TSAETWILTE KSEVGTGCTS SEQCGLFSTC LNGGICVDIW
NKRKCTCPIG FTGENCEENV NDCKYVDCGK NGYCLDGIDD AKCVCNNGFS GEHCEHANDE
CEGIECHNGG KCVKNGEKVT CKCEKQWMGD YCNVTMTTSC KDSPCQNFGQ CMQKTDSSFE
CNCMDGYSGQ LCEQRNVNEC NHYDCNRGHC VMTVSGPACQ CELGYTGRFC EKLLNHCSSN
TCSSRGTCSP VWNNTVCACD NNWRGSHCQY QTNACLDFPC GNDGVCRTNE GNTFTCECQK
FFMGTRCEIE GSCLKANCVH GECIQLSPER HTCSCNIGYE GDSCDHRIDY CKAGPCMNGA
SCENKLTGYK CSCSVGFEGA DCEINIDECA LGYCKNGAKC RDKINDYECV CDGTGYEGRN
CTTDINECEN PNNCINGECS NTLGGYKCTC KNGFIGPRCS MRNPCTAQIA SNNISSVTCV
HGKCVNPVVH IDKNREVAKY ECACDRGYTG PTCSQRIKES AMSNISYLFG PIIAVVIVFA
ILGCLLLLFV IRGNNAMHGH YSPSSHEFTQ NRMAMPTVIK LPPQERLI
//
