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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
 
 
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