IGDC4_HUMAN
ID IGDC4_HUMAN Reviewed; 1250 AA.
AC Q8TDY8; Q9HCE4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Immunoglobulin superfamily DCC subclass member 4;
DE AltName: Full=Neighbor of punc e11;
DE AltName: Full=Protein DDM36;
DE Short=hDDM36;
DE Flags: Precursor;
GN Name=IGDCC4; Synonyms=DDM36, KIAA1628, NOPE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Murakami H., Nakamata T., Nakayama T., Yamamoto H., Hosaka T., Aoyama T.,
RA Nagayama S., Oka M., Kiyono T., Sasaki M.S., Nakamura T., Toguchida J.;
RT "Up-regulation of a ras effector and down-regulation of a cell adhesion
RT molecule are associated with transformation of osteoblasts.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TDY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDY8-2; Sequence=VSP_028046;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; AB052622; BAB86306.1; -; mRNA.
DR EMBL; AB046848; BAB13454.1; -; mRNA.
DR CCDS; CCDS10206.1; -. [Q8TDY8-1]
DR RefSeq; NP_066013.1; NM_020962.2. [Q8TDY8-1]
DR AlphaFoldDB; Q8TDY8; -.
DR SMR; Q8TDY8; -.
DR BioGRID; 121745; 40.
DR IntAct; Q8TDY8; 3.
DR STRING; 9606.ENSP00000319623; -.
DR GlyConnect; 1944; 11 N-Linked glycans (6 sites).
DR GlyGen; Q8TDY8; 9 sites, 12 N-linked glycans (6 sites).
DR iPTMnet; Q8TDY8; -.
DR PhosphoSitePlus; Q8TDY8; -.
DR BioMuta; IGDCC4; -.
DR DMDM; 74760490; -.
DR jPOST; Q8TDY8; -.
DR MassIVE; Q8TDY8; -.
DR PaxDb; Q8TDY8; -.
DR PeptideAtlas; Q8TDY8; -.
DR PRIDE; Q8TDY8; -.
DR ProteomicsDB; 74374; -. [Q8TDY8-1]
DR ProteomicsDB; 74375; -. [Q8TDY8-2]
DR Antibodypedia; 2317; 66 antibodies from 13 providers.
DR DNASU; 57722; -.
DR Ensembl; ENST00000352385.3; ENSP00000319623.3; ENSG00000103742.12. [Q8TDY8-1]
DR GeneID; 57722; -.
DR KEGG; hsa:57722; -.
DR MANE-Select; ENST00000352385.3; ENSP00000319623.3; NM_020962.3; NP_066013.1.
DR UCSC; uc002aou.2; human. [Q8TDY8-1]
DR CTD; 57722; -.
DR DisGeNET; 57722; -.
DR GeneCards; IGDCC4; -.
DR HGNC; HGNC:13770; IGDCC4.
DR HPA; ENSG00000103742; Tissue enhanced (brain, skeletal muscle, tongue).
DR neXtProt; NX_Q8TDY8; -.
DR OpenTargets; ENSG00000103742; -.
DR PharmGKB; PA164720914; -.
DR VEuPathDB; HostDB:ENSG00000103742; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000159637; -.
DR HOGENOM; CLU_006906_0_0_1; -.
DR InParanoid; Q8TDY8; -.
DR OMA; WDVGPIR; -.
DR OrthoDB; 1010015at2759; -.
DR PhylomeDB; Q8TDY8; -.
DR TreeFam; TF321506; -.
DR PathwayCommons; Q8TDY8; -.
DR SignaLink; Q8TDY8; -.
DR BioGRID-ORCS; 57722; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; IGDCC4; human.
DR GenomeRNAi; 57722; -.
DR Pharos; Q8TDY8; Tbio.
DR PRO; PR:Q8TDY8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TDY8; protein.
DR Bgee; ENSG00000103742; Expressed in corpus epididymis and 157 other tissues.
DR Genevisible; Q8TDY8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 9.
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 Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1250
FT /note="Immunoglobulin superfamily DCC subclass member 4"
FT /id="PRO_0000304622"
FT TOPO_DOM 25..957
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 979..1250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..137
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 242..330
FT /note="Ig-like C2-type 3"
FT DOMAIN 335..421
FT /note="Ig-like C2-type 4"
FT DOMAIN 431..525
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 527..623
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 632..741
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 752..845
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 850..945
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1140..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 995
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 265..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 356..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..331
FT /note="MARGDAGRGRGLLALTFCLLAARGELLLPQETTVELSCGVGPLQVILGPEQA
FT AVLNCSLGAAAAGPPTRVTWSKDGDTLLEHDHLHLLPNGSLWLSQPLAPNGSDESVPEA
FT VGVIEGNYSCLAHGPLGVLASQTAVVKLATLADFSLHPESQTVEENGTARFECHIEGLP
FT APIITWEKDQVTLPEEPRLIVLPNGVLQILDVQESDAGPYRCVATNSARQHFSQEALLS
FT VAHRGSLASTRGQDVVIVAAPENTTVVSGQSVVMECVASADPTPFVSWVRQDGKPISTD
FT VIVLGRTNLLIANAQPWHSGVYVCRANKPRTRDFATAAAELRV -> MGRRKGRSALSR
FT SSLERVNQGEVKVIGRGAREGGGGQAWGTGGGGRDLSCGIPRSASPLAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_028046"
FT VARIANT 52
FT /note="A -> P (in dbSNP:rs34355056)"
FT /id="VAR_049966"
FT VARIANT 301
FT /note="N -> S (in dbSNP:rs12442757)"
FT /id="VAR_049967"
FT VARIANT 803
FT /note="S -> C (in dbSNP:rs1469778)"
FT /id="VAR_059391"
FT VARIANT 1102
FT /note="T -> A (in dbSNP:rs33918653)"
FT /id="VAR_049968"
FT VARIANT 1125
FT /note="C -> Y (in dbSNP:rs33918653)"
FT /id="VAR_049969"
SQ SEQUENCE 1250 AA; 134210 MW; 181CA412E935F977 CRC64;
MARGDAGRGR GLLALTFCLL AARGELLLPQ ETTVELSCGV GPLQVILGPE QAAVLNCSLG
AAAAGPPTRV TWSKDGDTLL EHDHLHLLPN GSLWLSQPLA PNGSDESVPE AVGVIEGNYS
CLAHGPLGVL ASQTAVVKLA TLADFSLHPE SQTVEENGTA RFECHIEGLP APIITWEKDQ
VTLPEEPRLI VLPNGVLQIL DVQESDAGPY RCVATNSARQ HFSQEALLSV AHRGSLASTR
GQDVVIVAAP ENTTVVSGQS VVMECVASAD PTPFVSWVRQ DGKPISTDVI VLGRTNLLIA
NAQPWHSGVY VCRANKPRTR DFATAAAELR VLAAPAITQA PEALSRTRAS TARFVCRASG
EPRPALRWLH NGAPLRPNGR VKVQGGGGSL VITQIGLQDA GYYQCVAENS AGMACAAASL
AVVVREGLPS APTRVTATPL SSSAVLVAWE RPEMHSEQII GFSLHYQKAR GMDNVEYQFA
VNNDTTELQV RDLEPNTDYE FYVVAYSQLG ASRTSTPALV HTLDDVPSAA PQLSLSSPNP
SDIRVAWLPL PPSLSNGQVV KYKIEYGLGK EDQIFSTEVR GNETQLMLNS LQPNKVYRVR
ISAGTAAGFG APSQWMHHRT PSMHNQSHVP FAPAELKVQA KMESLVVSWQ PPPHPTQISG
YKLYWREVGA EEEANGDRLP GGRGDQAWDV GPVRLKKKVK QYELTQLVPG RLYEVKLVAF
NKHEDGYAAV WKGKTEKAPA PDMPIQRGPP LPPAHVHAES NSSTSIWLRW KKPDFTTVKI
VNYTVRFSPW GLRNASLVTY YTSSGEDILI GGLKPFTKYE FAVQSHGVDM DGPFGSVVER
STLPDRPSTP PSDLRLSPLT PSTVRLHWCP PTEPNGEIVE YLILYSSNHT QPEHQWTLLT
TQGNIFSAEV HGLESDTRYF FKMGARTEVG PGPFSRLQDV ITLQEKLSDS LDMHSVTGII
VGVCLGLLCL LACMCAGLRR SPHRESLPGL SSTATPGNPA LYSRARLGPP SPPAAHELES
LVHPHPQDWS PPPSDVEDRA EVHSLMGGGV SEGRSHSKRK ISWAQPSGLS WAGSWAGCEL
PQAGPRPALT RALLPPAGTG QTLLLQALVY DAIKGNGRKK SPPACRNQVE AEVIVHSDFS
ASNGNPDLHL QDLEPEDPLP PEAPDLISGV GDPGQGAAWL DRELGGCELA APGPDRLTCL
PEAASASCSY PDLQPGEVLE ETPGDSCQLK SPCPLGASPG LPRSPVSSSA