NEO1_RAT
ID NEO1_RAT Reviewed; 1377 AA.
AC P97603;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Neogenin;
DE Flags: Precursor; Fragment;
GN Name=Neo1; Synonyms=Ngn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8861902; DOI=10.1016/s0092-8674(00)81336-7;
RA Keino-Masu K., Masu M., Hinck L., Leonardo E.D., Chan S.S.-Y.,
RA Culotti J.G., Tessier-Lavigne M.;
RT "Deleted in colorectal cancer (DCC) encodes a netrin receptor.";
RL Cell 87:175-185(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163; SER-1348 AND SER-1351,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Multi-functional cell surface receptor regulating cell
CC adhesion in many diverse developmental processes, including neural tube
CC and mammary gland formation, myogenesis and angiogenesis. Receptor for
CC members of the BMP, netrin, and repulsive guidance molecule (RGM)
CC families. Netrin-Neogenin interactions result in a chemoattractive axon
CC guidance response and cell-cell adhesion, the interaction between
CC NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYO10 (By similarity). Interacts with RGMA and
CC RGMB. Interacts with BMP2, BMP4, BMP6, and BMP7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: The Fibronectin repeats 5 and 6 mediate interaction with RGM
CC family molecules. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; U68726; AAB41100.1; -; mRNA.
DR AlphaFoldDB; P97603; -.
DR BMRB; P97603; -.
DR SMR; P97603; -.
DR STRING; 10116.ENSRNOP00000060347; -.
DR GlyGen; P97603; 8 sites, 3 N-linked glycans (1 site).
DR iPTMnet; P97603; -.
DR PhosphoSitePlus; P97603; -.
DR SwissPalm; P97603; -.
DR jPOST; P97603; -.
DR UCSC; RGD:619837; rat.
DR RGD; 619837; Neo1.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; P97603; -.
DR PhylomeDB; P97603; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0097708; C:intracellular vesicle; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098797; C:plasma membrane protein complex; ISO:RGD.
DR GO; GO:0070700; F:BMP receptor binding; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0039706; F:co-receptor binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0048679; P:regulation of axon regeneration; ISO:RGD.
DR GO; GO:2001222; P:regulation of neuron migration; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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; 2.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF06583; Neogenin_C; 2.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL <1..2
FT /evidence="ECO:0000255"
FT CHAIN 3..1377
FT /note="Neogenin"
FT /id="PRO_0000015045"
FT TOPO_DOM 3..1074
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..114
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..206
FT /note="Ig-like C2-type 2"
FT DOMAIN 198..305
FT /note="Ig-like C2-type 3"
FT DOMAIN 310..395
FT /note="Ig-like C2-type 4"
FT DOMAIN 410..504
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 510..600
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 605..700
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 710..800
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 825..924
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 926..1023
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1010..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97798"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 142..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 239..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 331..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 1377 AA; 150638 MW; E514ED8ABD1A63A9 CRC64;
AAAKNGSPPQ SAGASVRTFT PLYFLVEPVD TLSVRGSSVI LNCSAYSEPS PNIEWKKDGT
FLNLVSDDRR QLLPDGSLFI SNVVHSKHNK PDEGFYQCVA TVDNLGTIVS RTAKLAVAGL
PRFTSQPEPS SIYVGNSGIL NCEVNADLVP FVRWEQNRQP LLLDDRIVKL PSGTLVISNA
TEGDEGLYRC IVESGGPPKF SDEAELKVLQ ESEEMLDLVF LMRPSSMIKV IGQSAVLPCV
ASGLPAPVIR WMKNEDVLDT ESSGRLALLA GGSLEISDVT EDDAGTYFCV ADNGNKTIEA
QAELTVQVPP EFLKQPANIY ARESMDIVFE CEVTGKPAPT VKWVKNGDVV IPSDYFKIVK
EHNLQVLGLV KSDEGFYQCI AENDVGNAQA GAQLIILEHA PATTGPLPSA PRDVVASLVS
TRFIKLTWRT PASDPHGDNL TYSVFYTKEG VARERVENTS QPGEMQVTIQ NLMPATVYIF
KVMAQNKHGS GESSAPLRVE TQPEVQLPGP APNIRAYATS PTSITVTWET PLSGNGEIQN
YKLYYMEKGT DKEQDVDVSS HSYTINGLKK YTEYSFRVVA YNKHGPGVST QDVAVRTLSD
VPSAAPQNLS LEVRNSKSIV IHWQPPSSAT QNGQITGYKI RYRKASRKSD VTETVVTGTQ
LSQLIEGLDR GTEYNFRVAA LTVNGTGPAT DWLSAETFES DLDESRVPEV PSSLHVRPLV
TSIVVSWTPP ENQNIVVRGY AIGYGIGSPH AQTIKVDYKQ RYYTIENLDP SSHYVITLKA
FNNVGEGIPL YESAVTRPHT DTSEVDLFVI NAPYTPVPDP TPMMPPVGVQ ASILSHDTIR
ITWADNSLPK HQKITDSRYY TVRWKTNIPA NTKYKNANAT TLSYLVTGLK PNTLYEFSVM
VTKGRRSSTW SMTAHGATFE LVPTSPPKDV TVVSKEGKPR TIIVNWQPPS EANGKITGYI
IYYSTDVNAE IHDWVIEPVV GNRLTHQIQE LTLDTPYYFK IQARNSKGMG PMSEAVQFRT
PKADSSDKMP NDQALGSAGK GGRLPDLGSD YKPPMSGSNS PHGSPTSPLD SNMLLVIIVS
IGVITIVVVV IIAVFCTRRT TSHQKKKRAA CKSVNGSHKY KGNCKDVKPP DLWIHHERLE
LKPIDKSPDP NPVMTDTPIP RNSQDITPVD NSMDSNIHQR RNSYRGHESE DSMSTLAGRR
GMRPKMMMPF DSQPPQQSVR NTPSTDTMPA SSSQTCCTDH QDPEGATSSS YLASSQEEDS
GQSLPTAHVR PSHPLKSFAV PAIPPPGPPI YDPALPSTPL LSQQALNHHL HSVKTASIGT
LGRSRPPMPV VVPSAPEVQE ATRMLEDSES SYEPDELTKE MAHLEGLMKD LNAITTA
