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CLC14_MOUSE
ID   CLC14_MOUSE             Reviewed;         459 AA.
AC   Q8VCP9; Q3TP72; Q9CXA8; Q9D624; Q9DC55;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=C-type lectin domain family 14 member A;
DE   Flags: Precursor;
GN   Name=Clec14a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic lung, Head, Lung, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AK004557; BAB23370.2; -; mRNA.
DR   EMBL; AK014681; BAB29502.1; -; mRNA.
DR   EMBL; AK018432; BAB31209.1; -; mRNA.
DR   EMBL; AK033733; BAC28454.1; -; mRNA.
DR   EMBL; AK045596; BAC32430.1; -; mRNA.
DR   EMBL; AK080201; BAC37846.1; -; mRNA.
DR   EMBL; AK164665; BAE37865.1; -; mRNA.
DR   EMBL; BC019452; AAH19452.1; -; mRNA.
DR   CCDS; CCDS25930.1; -.
DR   RefSeq; NP_080085.3; NM_025809.5.
DR   AlphaFoldDB; Q8VCP9; -.
DR   SMR; Q8VCP9; -.
DR   STRING; 10090.ENSMUSP00000054451; -.
DR   GlyGen; Q8VCP9; 4 sites.
DR   iPTMnet; Q8VCP9; -.
DR   PhosphoSitePlus; Q8VCP9; -.
DR   MaxQB; Q8VCP9; -.
DR   PaxDb; Q8VCP9; -.
DR   PeptideAtlas; Q8VCP9; -.
DR   PRIDE; Q8VCP9; -.
DR   ProteomicsDB; 279098; -.
DR   Antibodypedia; 23322; 203 antibodies from 29 providers.
DR   DNASU; 66864; -.
DR   Ensembl; ENSMUST00000062254; ENSMUSP00000054451; ENSMUSG00000045930.
DR   GeneID; 66864; -.
DR   KEGG; mmu:66864; -.
DR   UCSC; uc007npv.2; mouse.
DR   CTD; 161198; -.
DR   MGI; MGI:1914114; Clec14a.
DR   VEuPathDB; HostDB:ENSMUSG00000045930; -.
DR   eggNOG; ENOG502S0KN; Eukaryota.
DR   GeneTree; ENSGT00930000151088; -.
DR   HOGENOM; CLU_593913_0_0_1; -.
DR   InParanoid; Q8VCP9; -.
DR   OMA; EMRCHLR; -.
DR   OrthoDB; 747312at2759; -.
DR   PhylomeDB; Q8VCP9; -.
DR   TreeFam; TF330714; -.
DR   BioGRID-ORCS; 66864; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q8VCP9; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8VCP9; protein.
DR   Bgee; ENSMUSG00000045930; Expressed in brain blood vessel and 178 other tissues.
DR   Genevisible; Q8VCP9; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO: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; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
DR   GO; GO:0001946; P:lymphangiogenesis; IMP:MGI.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:MGI.
DR   GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IMP:MGI.
DR   GO; GO:0036325; P:vascular endothelial growth factor receptor-3 signaling pathway; IMP:MGI.
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   Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..459
FT                   /note="C-type lectin domain family 14 member A"
FT                   /id="PRO_0000017378"
FT   TOPO_DOM        22..386
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        408..459
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          246..288
FT                   /note="EGF-like"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        30
FT                   /note="A -> R (in Ref. 1; BAB31209)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="T -> P (in Ref. 1; BAB23370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="T -> A (in Ref. 2; AAH19452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="I -> V (in Ref. 2; AAH19452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="S -> C (in Ref. 1; BAB23370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  49066 MW;  A257B38DA598EC8A CRC64;
     MRPALALCLL CPAFWPRPGN GEHPTADRAA CSASGACYSL HHATFKRRAA EEACSLRGGT
     LSTVHSGSEF QAVLLLLRAG PGPGGGSKDL LFWVALERSI SQCTQEKEPL RGFSWLHPDS
     EDSEDSPLPW VEEPQRSCTV RKCAALQATR GVEPAGWKEM RCHLRTDGYL CKYQFEVLCP
     APRPGAASNL SFQAPFRLSS SALDFSPPGT EVSAMCPGDL SVSSTCIQEE TSAHWDGLFP
     GTVLCPCSGR YLLAGKCVEL PDCLDHLGDF TCECAVGFEL GKDGRSCETK VEEQLTLEGT
     KLPTRNVTAT PAGAVTNRTW PGQVYDKPGE MPQVTEILQW GTQSTLPTIQ KTPQTKPKVT
     GTPSGSVVLN YTSSPPVSLT FDTSSTVVFI LVSIAVIVLV VLTITVLGLF KLCFHKSRSS
     RTGKGALDSP GVECDAEATS LHHSSTQCTD IGVKSGTVA
 
 
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