ID F4W5X3_ACREC Unreviewed; 1488 AA.
AC F4W5X3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Neogenin {ECO:0000313|EMBL:EGI70449.1};
GN ORFNames=G5I_00823 {ECO:0000313|EMBL:EGI70449.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70449.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000256|ARBA:ARBA00009588}.
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DR EMBL; GL887695; EGI70449.1; -; Genomic_DNA.
DR RefSeq; XP_011058279.1; XM_011059977.1.
DR STRING; 103372.F4W5X3; -.
DR EnsemblMetazoa; XM_011059977.1; XP_011058279.1; LOC105148316.
DR GeneID; 105148316; -.
DR KEGG; aec:105148316; -.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; F4W5X3; -.
DR OrthoDB; 5398621at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00063; FN3; 6.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF39; FI24025P1; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF06583; Neogenin_C; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1488
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003323350"
FT TRANSMEM 1121..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..117
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 124..212
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 225..315
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 318..403
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 503..594
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 600..689
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 694..794
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 804..894
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 904..1001
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1006..1103
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1189..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 164728 MW; F56D16BF9D818D56 CRC64;
MEPRPFTILL ALLLTTLARI NAGGLDFTIE PRDVVVEQGG SASLDCEAKS VLGTPSIQWR
TDDGQPITFI GDSYRSQLAN GSLYINSVYT GSAELIGSYQ CLASIDNVGA IVSRTATIKL
ASLPGFEREP QDTMVYAGQI AYLSCALPAS SSLLKIQWLK NEHPLVLDES RMTILPSGAL
EIDNVQYHDV GSYRCNASGY GQYRLSNKAQ LGLLSSDIDE GSSAPVFVAQ PLQQIVTEGS
DVTLECAANG YPKPSIFWLK DGVALDSTSQ DSRYHKVAAS SLVITNVRES DHGSYQCRAE
NMVDSLDAVA ELIVQVPPKF IKKPEDKIAS ESQDLEFECE IYGKPEPKIT WLKNGERITL
SAYWQIVNGY NLRINGLLPI DAGIFQCMGV NPAGSVQASA RLTINQPKRT NLYRTTPKTI
PKKKLLLHRQ LYNKTWQHPS TLLGHTFSSN MPNPPLSISP SDDPADLLPN SFKYPNPLYD
PNSRFVDDTD TLEAFDGGGI PSPPRNLSLV IVTARFVTLR WQEPENANSD ALNYFVYYKQ
EGAMRERVAN SLQKLEAMIR GLQPGMTYQF HVVAQNSRGT SAPSEVLQIT TLIEANVPGF
PMNLEGQPTS SMSITLSWEE PQVINGRISK YIITFMEGDG EEITRETTST TYELVDLVPY
TEYSIRVQAV NENGPGAFSK DIVIRTYSAQ PTQPPHNVTL EAASSTSIII RWEPPLEGQN
GIITGYRIRY RRYPHDSRAG DRRSPITVTT EGNQRLYVLT GLEKHVVYQV RICAFNVNGT
GPWTEWTKIE TYENDLDETK VPNAPSNLRA NAVADSILVS WHPPKDQSIK VRKYKLGWGK
GYPDVEIQVL DGKQRSYAIK PIEPTMEYVI SLRATNNVGD GQPSYANVRT PERFVSEPTV
PLIPPVGLKA IVLSASTVVL YWTDTTLSKS QYITDSRYYV VRYAFYHHSS NPRYRYYNAT
DLNCMIHDLK PNTQYEFTVR LVKGKRSSPW SMVVLNQTQE AAPSTAPRDL IIQTIEDRPT
SVLLRWQPPK QPNGQITGYL IIYSTDNTKW DRDWLVEGVI GDKVDAVVKG LHPNTVYYFK
IQARNSKGYG PFSTTVSFKT PPNNGMDDEL HGRDGRSFSN LLIYIIVGLS IVFVTAISVV
IVVCCKCNPS SPDRKKGYMK DTSNQKTNIK PPDLWIHHDQ MELKALEKSS LNGEASTSGV
TSNTLPRSGN QEYNQDNIHG NSSSLDKRTY VPSYMGNTDE KCSTLSRQHS RGSHKSKLIT
LPIDSAPLHQ PIATATPIVN SSMSQPTIHT SCSDTSSVRQ NYPRTVAQYS LNRAHVTLEP
TPESSPDSCI PSSYEPLQNQ LSYGTSGQSY SGNTQYASGH YGNNTQPVSS AVGENNTSKR
LQGHPLKSFS VPAPPPQSAP STPAQQKHGV SHVTVRPTMS GSPYKKSQGS SSQLTKNRLA
SVSNPAHTSE EVERLKPSYS TEELNQEMAN LEGLMKDLNA ITASEFEC
//
