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CLC14_HUMAN
ID   CLC14_HUMAN             Reviewed;         490 AA.
AC   Q86T13; Q695G9; Q6PWT6; Q8N5V5;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=C-type lectin domain family 14 member A;
DE   AltName: Full=Epidermal growth factor receptor 5;
DE            Short=EGFR-5;
DE   Flags: Precursor;
GN   Name=CLEC14A; Synonyms=C14orf27, EGFR5; ORFNames=UNQ236/PRO269;
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].
RX   PubMed=15636369;
RA   Fu J.Q., Wang L., Chen W., Ci H.L., Li Y.P.;
RT   "Cloning and characterization of a novel human ceg1 gene cDNA.";
RL   Shi Yan Sheng Wu Xue Bao 37:409-417(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 22-36.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- INTERACTION:
CC       Q86T13; P27449: ATP6V0C; NbExp=3; IntAct=EBI-17710733, EBI-721179;
CC       Q86T13; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-17710733, EBI-12256978;
CC       Q86T13; O14493: CLDN4; NbExp=3; IntAct=EBI-17710733, EBI-9316372;
CC       Q86T13; O14569: CYB561D2; NbExp=3; IntAct=EBI-17710733, EBI-717654;
CC       Q86T13; P50402: EMD; NbExp=3; IntAct=EBI-17710733, EBI-489887;
CC       Q86T13; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-17710733, EBI-2820517;
CC       Q86T13; Q13021: MALL; NbExp=3; IntAct=EBI-17710733, EBI-750078;
CC       Q86T13; Q99735: MGST2; NbExp=3; IntAct=EBI-17710733, EBI-11324706;
CC       Q86T13; P11836: MS4A1; NbExp=3; IntAct=EBI-17710733, EBI-2808234;
CC       Q86T13; Q01453: PMP22; NbExp=3; IntAct=EBI-17710733, EBI-2845982;
CC       Q86T13; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-17710733, EBI-12887458;
CC       Q86T13; O60636: TSPAN2; NbExp=3; IntAct=EBI-17710733, EBI-3914288;
CC       Q86T13; Q15836: VAMP3; NbExp=3; IntAct=EBI-17710733, EBI-722343;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AY573061; AAS77882.1; -; mRNA.
DR   EMBL; AY606132; AAT92280.1; -; mRNA.
DR   EMBL; BX248017; CAD62342.1; -; mRNA.
DR   EMBL; AY358395; AAQ88761.1; -; mRNA.
DR   EMBL; AL161751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031567; AAH31567.2; -; mRNA.
DR   CCDS; CCDS9667.1; -.
DR   RefSeq; NP_778230.1; NM_175060.2.
DR   AlphaFoldDB; Q86T13; -.
DR   SMR; Q86T13; -.
DR   BioGRID; 127776; 89.
DR   IntAct; Q86T13; 18.
DR   STRING; 9606.ENSP00000353013; -.
DR   DrugBank; DB02709; Resveratrol.
DR   GlyGen; Q86T13; 4 sites, 3 O-linked glycans (2 sites).
DR   iPTMnet; Q86T13; -.
DR   PhosphoSitePlus; Q86T13; -.
DR   SwissPalm; Q86T13; -.
DR   BioMuta; CLEC14A; -.
DR   DMDM; 34582300; -.
DR   jPOST; Q86T13; -.
DR   MassIVE; Q86T13; -.
DR   PaxDb; Q86T13; -.
DR   PeptideAtlas; Q86T13; -.
DR   PRIDE; Q86T13; -.
DR   ProteomicsDB; 69656; -.
DR   Antibodypedia; 23322; 203 antibodies from 29 providers.
DR   DNASU; 161198; -.
DR   Ensembl; ENST00000342213.3; ENSP00000353013.2; ENSG00000176435.7.
DR   GeneID; 161198; -.
DR   KEGG; hsa:161198; -.
DR   MANE-Select; ENST00000342213.3; ENSP00000353013.2; NM_175060.3; NP_778230.1.
DR   UCSC; uc001wum.3; human.
DR   CTD; 161198; -.
DR   DisGeNET; 161198; -.
DR   GeneCards; CLEC14A; -.
DR   HGNC; HGNC:19832; CLEC14A.
DR   HPA; ENSG00000176435; Low tissue specificity.
DR   neXtProt; NX_Q86T13; -.
DR   OpenTargets; ENSG00000176435; -.
DR   PharmGKB; PA134890576; -.
DR   VEuPathDB; HostDB:ENSG00000176435; -.
DR   eggNOG; ENOG502S0KN; Eukaryota.
DR   GeneTree; ENSGT00930000151088; -.
DR   HOGENOM; CLU_593913_0_0_1; -.
DR   InParanoid; Q86T13; -.
DR   OMA; EMRCHLR; -.
DR   OrthoDB; 747312at2759; -.
DR   PhylomeDB; Q86T13; -.
DR   TreeFam; TF330714; -.
DR   PathwayCommons; Q86T13; -.
DR   SignaLink; Q86T13; -.
DR   BioGRID-ORCS; 161198; 12 hits in 1067 CRISPR screens.
DR   ChiTaRS; CLEC14A; human.
DR   GenomeRNAi; 161198; -.
DR   Pharos; Q86T13; Tbio.
DR   PRO; PR:Q86T13; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q86T13; protein.
DR   Bgee; ENSG00000176435; Expressed in apex of heart and 170 other tissues.
DR   Genevisible; Q86T13; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR   GO; GO:1990430; F:extracellular matrix protein binding; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0001946; P:lymphangiogenesis; IEA:Ensembl.
DR   GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IMP:GO_Central.
DR   GO; GO:0036325; P:vascular endothelial growth factor receptor-3 signaling pathway; IMP:GO_Central.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Lectin; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           22..490
FT                   /note="C-type lectin domain family 14 member A"
FT                   /id="PRO_0000017377"
FT   TOPO_DOM        22..397
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        419..490
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          33..173
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          245..287
FT                   /note="EGF-like"
FT   REGION          286..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        432
FT                   /note="Q -> H (in Ref. 1; AAS77882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="S -> F (in Ref. 1; AAS77882)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   490 AA;  51636 MW;  CE453A274CD39BF6 CRC64;
     MRPAFALCLL WQALWPGPGG GEHPTADRAG CSASGACYSL HHATMKRQAA EEACILRGGA
     LSTVRAGAEL RAVLALLRAG PGPGGGSKDL LFWVALERRR SHCTLENEPL RGFSWLSSDP
     GGLESDTLQW VEEPQRSCTA RRCAVLQATG GVEPAGWKEM RCHLRANGYL CKYQFEVLCP
     APRPGAASNL SYRAPFQLHS AALDFSPPGT EVSALCRGQL PISVTCIADE IGARWDKLSG
     DVLCPCPGRY LRAGKCAELP NCLDDLGGFA CECATGFELG KDGRSCVTSG EGQPTLGGTG
     VPTRRPPATA TSPVPQRTWP IRVDEKLGET PLVPEQDNSV TSIPEIPRWG SQSTMSTLQM
     SLQAESKATI TPSGSVISKF NSTTSSATPQ AFDSSSAVVF IFVSTAVVVL VILTMTVLGL
     VKLCFHESPS SQPRKESMGP PGLESDPEPA ALGSSSAHCT NNGVKVGDCD LRDRAEGALL
     AESPLGSSDA
 
 
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