MFA3L_RAT
ID MFA3L_RAT Reviewed; 409 AA.
AC Q6AYP2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Microfibrillar-associated protein 3-like;
DE Flags: Precursor;
GN Name=Mfap3l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-303; SER-306 AND
RP SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- CAUTION: A protein kinase activity has been reported kinase activity
CC however PROSITE, Pfam do not detect a protein kinase domain. Its enzyme
CC activity is therefore unsure. {ECO:0000250|UniProtKB:O75121}.
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DR EMBL; BC078969; AAH78969.1; -; mRNA.
DR RefSeq; NP_001012049.1; NM_001012049.1.
DR RefSeq; XP_017455596.1; XM_017600107.1.
DR AlphaFoldDB; Q6AYP2; -.
DR SMR; Q6AYP2; -.
DR STRING; 10116.ENSRNOP00000015759; -.
DR GlyGen; Q6AYP2; 5 sites.
DR iPTMnet; Q6AYP2; -.
DR PhosphoSitePlus; Q6AYP2; -.
DR PaxDb; Q6AYP2; -.
DR PRIDE; Q6AYP2; -.
DR Ensembl; ENSRNOT00000015759; ENSRNOP00000015759; ENSRNOG00000011775.
DR GeneID; 306424; -.
DR KEGG; rno:306424; -.
DR UCSC; RGD:1311274; rat.
DR CTD; 9848; -.
DR RGD; 1311274; Mfap3l.
DR eggNOG; ENOG502QW9J; Eukaryota.
DR GeneTree; ENSGT00390000011576; -.
DR HOGENOM; CLU_056017_2_0_1; -.
DR InParanoid; Q6AYP2; -.
DR OMA; GGKWWLL; -.
DR OrthoDB; 1154642at2759; -.
DR PhylomeDB; Q6AYP2; -.
DR TreeFam; TF333205; -.
DR PRO; PR:Q6AYP2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011775; Expressed in testis and 16 other tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
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; IEA:Ensembl.
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 Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW 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_0000014871"
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 REGION 319..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
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:22673903"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 409 AA; 45377 MW; E2AB63432ACD208F CRC64;
MGLLKSHLTV CLPPSVPFLI LVSTLATAKS VTNSTLNGTD VVLGSVPVII ARTDHIIVKE
GNSALINCSA FGIPDLEYKW YNSVGKLLKE MDDEKERGGG KWQMLDGGLL NITKVSFSDR
GKYTCVASNI YGTINNTVTL RVIFTSGDMG VYYMVVCLVA FTIVMILNIT RLCMMSSHLK
KTEKAINEFF RTEGAEKLQK AFEIAKRIPI ITSAKTLELA KVTQFKTMEF ARYIEELARS
VPLPPLIMNC RTIMEEIMEV VGLEEQGQNF VRHTPEGQEA PDRDEVYTIP NSLKRSESPT
ADSDASSLHE QPQQIAIKVS VHPQSKKDHV DDQEGENLEV KDEEETEPSE EHSPETAEPS
TDITTTELTS EEASPVEAPE RELPPAHLET TEPAVTCDRN TCIIYESHV
