NEO1_CHICK
ID NEO1_CHICK Reviewed; 1443 AA.
AC Q90610;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Neogenin;
DE Flags: Fragment;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Embryonic brain;
RX PubMed=7806578; DOI=10.1083/jcb.127.6.2009;
RA Vielmetter J., Roman J.M., Dreyer W.J.;
RT "Neogenin, an avian cell surface protein expressed during terminal neuronal
RT differentiation, is closely related to the human tumor suppressor molecule
RT deleted in colorectal cancer.";
RL J. Cell Biol. 127:2009-2020(1994).
CC -!- FUNCTION: May be involved as a regulatory protein in the transition of
CC undifferentiated proliferating cells to their differentiated state. May
CC also function as a cell adhesion molecule in a broad spectrum of
CC embryonic and adult tissues.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DEVELOPMENTAL STAGE: In retina, expressed on ganglion cell fibers as
CC soon as they begin to extend their axons.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; U07644; AAC59662.1; -; mRNA.
DR PIR; I50600; I50600.
DR AlphaFoldDB; Q90610; -.
DR BMRB; Q90610; -.
DR SMR; Q90610; -.
DR IntAct; Q90610; 1.
DR STRING; 9031.ENSGALP00000034118; -.
DR PaxDb; Q90610; -.
DR PRIDE; Q90610; -.
DR VEuPathDB; HostDB:geneid_395822; -.
DR eggNOG; KOG4221; Eukaryota.
DR PhylomeDB; Q90610; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:InterPro.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 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; IPR033024; Neogenin.
DR InterPro; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF14; PTHR44170:SF14; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF06583; Neogenin_C; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..1443
FT /note="Neogenin"
FT /id="PRO_0000072707"
FT TOPO_DOM <1..1090
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 118..204
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..302
FT /note="Ig-like C2-type 3"
FT DOMAIN 307..392
FT /note="Ig-like C2-type 4"
FT DOMAIN 427..521
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 527..617
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..716
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 726..816
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 841..937
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 942..1039
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1026..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 236..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 328..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 1443 AA; 158051 MW; 558C6795579C0E26 CRC64;
RSGPRSPLTG SVVRTFTPFY FLVEPMDILS VRGASVIMNC SSYCETPPKI EWKKDGTLLN
LVSDDRRQLL PDGSLLINSV VHSKHNKPDE GYYQCVATVE SLGSIVSRTA KLTVAGLPRF
TSQPELSSVY KGNSAILNCE VNVDLAPFVR WEQDRQPLSL DDRVFKLPSG ALLIGNATDT
DGGFYRCVIE SGGTPKYSEE AELKILPDPE EPQSLVFVRQ PSSLTKVTGQ NAVFPCVAGG
FPTPYVRWTK NGEELITEDS ERFALRAGGS LLISDVTEED VGTYTCIADN ENETIEAQAE
LAVQVPPEFL KRPANIYAHE SMDIVFECEV TGKPTPTVKW VKNGDVVIPS DYFKIVKEHN
LQVLGLVKSD EGFYQCIAEN DVGNAQAGAQ LIILDLDVAI PTLPPTSLTS ATNDHLAPAT
TGPLPTAPRD VVATLVSTRF IRLTWRTPVS DPQGDNLTYS IFYTKEGINR ERVENTSRPG
ETQVMIQNLM PETVYVFRVV AQNKHGHGES SAPLKVATQP EVQLPGPAPN IRAYAGSPTS
VTVTWETPLS GNGEIQNYKL YYMEKGQDSE QDVDVAGLSY TITGLKKYTE YSFRVVAYNK
HGPGVSTQDV VVRTLSDVPS AAPQNLTLEA RNSKSIMLHW QPPPAGTHSG QITGYKIRYR
KVSRKSDVTE SVGGTQLFQL IEGLERGTEY NFRIAAMTVN GTGPATDWVS AETFESDLDE
SRVPEVPSSL HVRPLVTSIV VSWTPPENQN IVVRGYAIGY GIGSPHAQTI KVDYKQRYYT
IENLDPSSHY VITLKAFNNV GEGIPLYESA VTRPHSDTSE VDLFVINAPY TPVPDPSPMM
PPVGVQASIL SHDTIRITWA DNSLPKNQKI TDARYYTVRW KTNIPANTKY KTANATTLSY
LVTGLKPNTL YEFSVMVTKG RRSSTWSMTA HGTTFELVPT SPPKDVTVVS KEGKPRTIIV
NWQPPSEANG KITGYIIYYS TDVNAEIHDW VIEPVVGNRL THQIQELTLD TPYYFKIQAR
NSKGMGPMSE AVQFRTPKAE SSDKMPNDQA SGSAGKGSRP VDVGPDYKPP LSGSNSPHGS
PTSPLDSNML LVIIVSVGVI TIVIVVIVAV FCTRRTTSHQ KKKRAACKSV NGSHKYKGNS
KDVKPPDLWI HHERLELKPI DKSPDPNPIM TDTPIPRNSQ DITPVDNSMD SNIHQRRNSY
RGHESEDSMS TLAGRRGMRP KMMMPFDSQP PQPVISAHPI HSLDNPHHHF HSGSLASPTR
SYLHHQVSPW PVGTSMSHSD RANSTESVRN TPSSDTMPAS SSQPCADHQD PDSSSGAYLG
SAQEEDAAQS LPTAHVRPSH PLKSFAVPAV PAAGSAYDPT LPSTPLLTQQ APSHPVHSVK
TASIGTLGRT RPPMPVVVPS APDVQETTRM LEDSESSYEP DELTKEMAHL EGLMKDLNAI
TTA
