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Database: UniProt
Entry: Q8K5B2
LinkDB: Q8K5B2
Original site: Q8K5B2 
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   27-MAR-2024, entry version 145.
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.ENSMUSP00000024963; -.
DR   iPTMnet; Q8K5B2; -.
DR   PhosphoSitePlus; Q8K5B2; -.
DR   EPD; Q8K5B2; -.
DR   jPOST; Q8K5B2; -.
DR   MaxQB; Q8K5B2; -.
DR   PaxDb; 10090-ENSMUSP00000121820; -.
DR   PeptideAtlas; Q8K5B2; -.
DR   ProteomicsDB; 295706; -.
DR   Pumba; Q8K5B2; -.
DR   Antibodypedia; 29996; 219 antibodies from 29 providers.
DR   DNASU; 193813; -.
DR   Ensembl; ENSMUST00000024963.11; ENSMUSP00000024963.4; ENSMUSG00000024150.13.
DR   Ensembl; ENSMUST00000129616.8; ENSMUSP00000123352.2; ENSMUSG00000024150.13.
DR   Ensembl; ENSMUST00000144236.9; ENSMUSP00000121820.2; ENSMUSG00000024150.13.
DR   GeneID; 193813; -.
DR   KEGG; mmu:193813; -.
DR   UCSC; uc008dur.2; mouse.
DR   AGR; MGI:2183439; -.
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; PESHRPN; -.
DR   OrthoDB; 2882831at2759; -.
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 76 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 270 other cell types or 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23104:SF14; MULTIPLE COAGULATION FACTOR DEFICIENCY PROTEIN 2; 1.
DR   PANTHER; PTHR23104; MULTIPLE COAGULATION FACTOR DEFICIENCY PROTEIN 2 NEURAL STEM CELL DERIVED NEURONAL SURVIVAL PROTEIN; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SUPFAM; SSF47473; EF-hand; 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
//
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