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MFA3L_MOUSE
ID   MFA3L_MOUSE             Reviewed;         409 AA.
AC   Q9D3X9; Q80TV6; Q8BJA9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Microfibrillar-associated protein 3-like;
DE   Flags: Precursor;
GN   Name=Mfap3l; Synonyms=Kiaa0626;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 1).
RC   TISSUE=Mammary gland;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-409 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-303 AND SER-306, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
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   -!- FUNCTION: May participate in the nuclear signaling of EGFR and
CC       MAPK1/ERK2. {ECO:0000250|UniProtKB:O75121}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75121};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75121}.
CC       Nucleus {ECO:0000250|UniProtKB:O75121}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O75121}. Note=Mainly localized in the nucleus.
CC       {ECO:0000250|UniProtKB:O75121}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D3X9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D3X9-2; Sequence=VSP_014096;
CC   -!- CAUTION: A protein kinase activity has been reported however PROSITE,
CC       Pfam do not detect a protein kinase domain. Its enzyme activity is
CC       therefore unsure. {ECO:0000250|UniProtKB:O75121}.
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DR   EMBL; AK016959; BAB30523.1; -; mRNA.
DR   EMBL; AK089654; BAC40939.1; -; mRNA.
DR   EMBL; BC095950; AAH95950.1; -; mRNA.
DR   EMBL; AK122332; BAC65614.1; -; mRNA.
DR   CCDS; CCDS22321.1; -. [Q9D3X9-1]
DR   CCDS; CCDS80877.1; -. [Q9D3X9-2]
DR   RefSeq; NP_001171352.1; NM_001177881.1. [Q9D3X9-1]
DR   RefSeq; NP_001171353.1; NM_001177882.1. [Q9D3X9-1]
DR   RefSeq; NP_001280698.1; NM_001293769.1. [Q9D3X9-2]
DR   RefSeq; NP_082032.1; NM_027756.5. [Q9D3X9-1]
DR   AlphaFoldDB; Q9D3X9; -.
DR   IntAct; Q9D3X9; 1.
DR   STRING; 10090.ENSMUSP00000125139; -.
DR   GlyGen; Q9D3X9; 5 sites.
DR   iPTMnet; Q9D3X9; -.
DR   PhosphoSitePlus; Q9D3X9; -.
DR   SwissPalm; Q9D3X9; -.
DR   MaxQB; Q9D3X9; -.
DR   PaxDb; Q9D3X9; -.
DR   PeptideAtlas; Q9D3X9; -.
DR   PRIDE; Q9D3X9; -.
DR   ProteomicsDB; 295558; -. [Q9D3X9-1]
DR   ProteomicsDB; 295559; -. [Q9D3X9-2]
DR   Antibodypedia; 17138; 105 antibodies from 20 providers.
DR   DNASU; 71306; -.
DR   Ensembl; ENSMUST00000034066; ENSMUSP00000034066; ENSMUSG00000031647. [Q9D3X9-1]
DR   Ensembl; ENSMUST00000160719; ENSMUSP00000125139; ENSMUSG00000031647. [Q9D3X9-1]
DR   Ensembl; ENSMUST00000161421; ENSMUSP00000124136; ENSMUSG00000031647. [Q9D3X9-2]
DR   Ensembl; ENSMUST00000161702; ENSMUSP00000124330; ENSMUSG00000031647. [Q9D3X9-1]
DR   GeneID; 71306; -.
DR   KEGG; mmu:71306; -.
DR   UCSC; uc009ltf.3; mouse. [Q9D3X9-1]
DR   CTD; 9848; -.
DR   MGI; MGI:1918556; Mfap3l.
DR   VEuPathDB; HostDB:ENSMUSG00000031647; -.
DR   eggNOG; ENOG502QW9J; Eukaryota.
DR   GeneTree; ENSGT00390000011576; -.
DR   HOGENOM; CLU_056017_2_0_1; -.
DR   InParanoid; Q9D3X9; -.
DR   OMA; GGKWWLL; -.
DR   OrthoDB; 1154642at2759; -.
DR   PhylomeDB; Q9D3X9; -.
DR   TreeFam; TF333205; -.
DR   BioGRID-ORCS; 71306; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Mfap3l; mouse.
DR   PRO; PR:Q9D3X9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9D3X9; protein.
DR   Bgee; ENSMUSG00000031647; Expressed in lacrimal gland and 215 other tissues.
DR   Genevisible; Q9D3X9; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
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; IPR039696; MFAP3-like.
DR   PANTHER; PTHR14340; PTHR14340; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..409
FT                   /note="Microfibrillar-associated protein 3-like"
FT                   /id="PRO_0000014870"
FT   TOPO_DOM        29..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..141
FT                   /note="Ig-like C2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          319..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         287
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O75121"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYP2"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..103
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014096"
FT   CONFLICT        283
FT                   /note="R -> G (in Ref. 1; BAC40939)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45342 MW;  BC0B3FA7568AA4C8 CRC64;
     MGLQKSHLTV CLPPSVPFLI LVSTLATAKS VTNSTLNGTD VVLGSVPVII ARTDHIIVKE
     GSSALINCSA YGFPDLEFKW YNSVGKLLKE MDDEKEKGGG KWQMLDGGLL NITKVSFSDR
     GKYTCVASNI YGTINNTVTL RVIFTSGDMG VYYMVVCLVA FTIVMILNIT RLCMMSSHLK
     KTEKAINEFF RTEGAEKLQK AFEIAKRIPI ITSAKTLELA KVTQFKTMEF ARYIEELARS
     VPLPPLIMNC RTIMEEIMEV VGLEEQGQNF VRHTPEGQEA PDRDEVYTIP NSLKRSESPT
     ADSDASSLHE QPQQIAIKVS VHPQSKRDHV DDQEGGHFEV KDEEETEPSE EHSPETAEPS
     TDITTTELTS EETSPVEAPE RGLPPAHLET TEPAVTCDRN TCIIYESHV
 
 
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