MCFD2_MOUSE
ID MCFD2_MOUSE Reviewed; 145 AA.
AC Q8K5B2; Q3U9G5;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Multiple coagulation factor deficiency protein 2 homolog;
DE AltName: Full=Neural stem cell-derived neuronal survival protein;
DE Flags: Precursor;
GN Name=Mcfd2; Synonyms=Sdnsf;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Toda H., Tashiro K., Takahashi J., Hashimoto N., Nakano I., Kobuke K.,
RA Tsuji M., Honjo T.;
RT "Isolation and characterization of SDNSF, a novel secretory molecule with
RT neuronal survival effect, from adult rat hippocampal stem cells.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Hippocampus, Pancreas, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC 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: The MCFD2-LMAN1 complex forms a specific cargo receptor for
CC the ER-to-Golgi transport of selected proteins. {ECO:0000250}.
CC -!- SUBUNIT: Interacts in a calcium-dependent manner with LMAN1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}.
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DR EMBL; AF475283; AAM28464.1; -; mRNA.
DR EMBL; AK033139; BAC28169.1; -; mRNA.
DR EMBL; AK075781; BAC35955.1; -; mRNA.
DR EMBL; AK077139; BAC36638.1; -; mRNA.
DR EMBL; AK077631; BAC36914.1; -; mRNA.
DR EMBL; AK141599; BAE24757.1; -; mRNA.
DR EMBL; AK151803; BAE30702.1; -; mRNA.
DR CCDS; CCDS29015.1; -.
DR RefSeq; NP_647456.1; NM_139295.3.
DR RefSeq; NP_789778.1; NM_176808.5.
DR RefSeq; XP_006523964.1; XM_006523901.3.
DR AlphaFoldDB; Q8K5B2; -.
DR SMR; Q8K5B2; -.
DR BioGRID; 228760; 4.
DR STRING; 10090.ENSMUSP00000121820; -.
DR iPTMnet; Q8K5B2; -.
DR PhosphoSitePlus; Q8K5B2; -.
DR EPD; Q8K5B2; -.
DR jPOST; Q8K5B2; -.
DR MaxQB; Q8K5B2; -.
DR PaxDb; Q8K5B2; -.
DR PeptideAtlas; Q8K5B2; -.
DR PRIDE; Q8K5B2; -.
DR ProteomicsDB; 295706; -.
DR Antibodypedia; 29996; 182 antibodies from 29 providers.
DR DNASU; 193813; -.
DR Ensembl; ENSMUST00000024963; ENSMUSP00000024963; ENSMUSG00000024150.
DR Ensembl; ENSMUST00000129616; ENSMUSP00000123352; ENSMUSG00000024150.
DR Ensembl; ENSMUST00000144236; ENSMUSP00000121820; ENSMUSG00000024150.
DR GeneID; 193813; -.
DR KEGG; mmu:193813; -.
DR UCSC; uc008dur.2; mouse.
DR CTD; 90411; -.
DR MGI; MGI:2183439; Mcfd2.
DR VEuPathDB; HostDB:ENSMUSG00000024150; -.
DR eggNOG; KOG4065; Eukaryota.
DR GeneTree; ENSGT00940000154141; -.
DR HOGENOM; CLU_100744_1_0_1; -.
DR InParanoid; Q8K5B2; -.
DR OMA; QDHIMEH; -.
DR OrthoDB; 1601131at2759; -.
DR PhylomeDB; Q8K5B2; -.
DR TreeFam; TF315801; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 193813; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Mcfd2; mouse.
DR PRO; PR:Q8K5B2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K5B2; protein.
DR Bgee; ENSMUSG00000024150; Expressed in parotid gland and 266 other tissues.
DR ExpressionAtlas; Q8K5B2; baseline and differential.
DR Genevisible; Q8K5B2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..145
FT /note="Multiple coagulation factor deficiency protein 2
FT homolog"
FT /id="PRO_0000004160"
FT DOMAIN 67..102
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 115..145
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K5B3"
SQ SEQUENCE 145 AA; 16168 MW; EB654BA9B76E0269 CRC64;
MATLQLLRAP LLCVLLWVFC APGARAHDHG ADVHHGSVGL DKSTVHDQEH IMEHLEGVID
QPEAEMSPQE LQLHYFKMHD YDGNSLLDGL ELSIAITHVH KEEGSEQAPV MSEDELVSII
DGVLRDDDKN NDGYIDYAEF AKSLQ
