ID MSPD2_MOUSE Reviewed; 518 AA.
AC Q9CWP6; Q8BYF8; Q8BZB6; Q8C0G1; Q8R0T7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 24-JAN-2024, entry version 156.
DE RecName: Full=Motile sperm domain-containing protein 2 {ECO:0000305};
GN Name=Mospd2 {ECO:0000312|MGI:MGI:1924013};
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; 2 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryonic stem cell, Fetal testis, and Thymus;
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 3), AND VARIANT SER-288.
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, 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).
RN [4]
RP STRUCTURE BY NMR OF 317-455.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the MSP domain of Riken cDNA 6030424E15.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Endoplasmic reticulum-anchored protein that mediates the
CC formation of contact sites between the endoplasmic (ER) and endosomes,
CC mitochondria or Golgi through interaction with conventional- and
CC phosphorylated-FFAT-containing organelle-bound proteins. In addition,
CC forms endoplasmic reticulum (ER)-lipid droplets (LDs) contacts through
CC a direct protein-membrane interaction and participates in LDs
CC homeostasis. The attachment mechanism involves an amphipathic helix
CC that has an affinity for lipid packing defects present at the surface
CC of LDs. Promotes migration of primary monocytes and neutrophils, in
CC response to various chemokines. {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- SUBUNIT: Homooligomer. Interacts (via MSP domain) with STARD3NL (via
CC FFAT motif), RMDN3 (via FFAT motif), OSBPL1A (via FFAT motif) and CERT1
CC (via FFAT motif). Interacts (via MSP domain) with STARD3 (via
CC phosphorylated FFAT motif); this interaction depends on the critical
CC phosphorylation of STARD3 on 'Ser-209'. Interacts with RB1CC1 (via
CC phosphorylated FFAT motif), MIGA2 (via phosphorylated FFAT motif) and
CC OSBPL1A (via FFAT motif). {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NHP6}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8NHP6}. Note=Localization to contact sites
CC involving the endoplasmic reticulum and several organelles is regulated
CC by interaction with proteins containing FFAT motif. Dynamically
CC distributes between specific subdomains of the endoplasmic reticulum
CC (ER): ER membranes in contact with lipid droplets (LDs) and the
CC remainder of the ER. {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CWP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWP6-2; Sequence=VSP_014050, VSP_014051;
CC Name=3;
CC IsoId=Q9CWP6-3; Sequence=VSP_014049, VSP_014052;
CC Name=4;
CC IsoId=Q9CWP6-4; Sequence=VSP_014047, VSP_014048;
CC -!- DOMAIN: The MSP domain is required for binding to the FFAT motif of
CC target proteins. {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- DOMAIN: The CRAL-TRIO domain is necessary for the recruitment to lipid
CC droplets (LDs) and mediates the formation of ER-LDs contacts through an
CC amphipathic helix. {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- DOMAIN: The transmembrane domain is necessary for binding to LDs.
CC {ECO:0000250|UniProtKB:Q8NHP6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29267.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK010480; BAB26972.1; -; mRNA.
DR EMBL; AK031405; BAC27389.1; -; mRNA.
DR EMBL; AK035985; BAC29267.1; ALT_FRAME; mRNA.
DR EMBL; AK039893; BAC30475.1; -; mRNA.
DR EMBL; BC026425; AAH26425.1; -; mRNA.
DR CCDS; CCDS53241.1; -. [Q9CWP6-1]
DR CCDS; CCDS72467.1; -. [Q9CWP6-3]
DR CCDS; CCDS72468.1; -. [Q9CWP6-2]
DR RefSeq; NP_001277452.1; NM_001290523.1. [Q9CWP6-3]
DR RefSeq; NP_001277453.1; NM_001290524.1. [Q9CWP6-2]
DR RefSeq; NP_084006.2; NM_029730.4.
DR PDB; 1WIC; NMR; -; A=317-455.
DR PDBsum; 1WIC; -.
DR AlphaFoldDB; Q9CWP6; -.
DR SMR; Q9CWP6; -.
DR IntAct; Q9CWP6; 1.
DR STRING; 10090.ENSMUSP00000004715; -.
DR iPTMnet; Q9CWP6; -.
DR PhosphoSitePlus; Q9CWP6; -.
DR SwissPalm; Q9CWP6; -.
DR MaxQB; Q9CWP6; -.
DR PaxDb; 10090-ENSMUSP00000004715; -.
DR PeptideAtlas; Q9CWP6; -.
DR ProteomicsDB; 291423; -. [Q9CWP6-1]
DR ProteomicsDB; 291424; -. [Q9CWP6-2]
DR ProteomicsDB; 291425; -. [Q9CWP6-3]
DR ProteomicsDB; 291426; -. [Q9CWP6-4]
DR Pumba; Q9CWP6; -.
DR Antibodypedia; 516; 90 antibodies from 16 providers.
DR Ensembl; ENSMUST00000112247.9; ENSMUSP00000107866.3; ENSMUSG00000061778.11. [Q9CWP6-2]
DR Ensembl; ENSMUST00000112248.9; ENSMUSP00000107867.3; ENSMUSG00000061778.11. [Q9CWP6-3]
DR GeneID; 76763; -.
DR KEGG; mmu:76763; -.
DR UCSC; uc009uvt.3; mouse. [Q9CWP6-3]
DR UCSC; uc009uvu.3; mouse. [Q9CWP6-2]
DR UCSC; uc009uvx.3; mouse. [Q9CWP6-4]
DR AGR; MGI:1924013; -.
DR CTD; 158747; -.
DR MGI; MGI:1924013; Mospd2.
DR VEuPathDB; HostDB:ENSMUSG00000061778; -.
DR eggNOG; KOG0439; Eukaryota.
DR eggNOG; KOG1470; Eukaryota.
DR GeneTree; ENSGT00390000016713; -.
DR HOGENOM; CLU_028924_1_0_1; -.
DR InParanoid; Q9CWP6; -.
DR OrthoDB; 2168468at2759; -.
DR PhylomeDB; Q9CWP6; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 76763; 0 hits in 77 CRISPR screens.
DR EvolutionaryTrace; Q9CWP6; -.
DR PRO; PR:Q9CWP6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CWP6; Protein.
DR Bgee; ENSMUSG00000061778; Expressed in parotid gland and 266 other cell types or tissues.
DR ExpressionAtlas; Q9CWP6; baseline and differential.
DR Genevisible; Q9CWP6; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; ISO:MGI.
DR GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0033149; F:FFAT motif binding; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR PANTHER; PTHR46384; MOTILE SPERM DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR46384:SF1; MOTILE SPERM DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF49354; PapD-like; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50202; MSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chemotaxis; Endoplasmic reticulum;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Motile sperm domain-containing protein 2"
FT /id="PRO_0000213464"
FT TOPO_DOM 1..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..518
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000250|UniProtKB:Q8NHP6"
FT DOMAIN 85..239
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 327..445
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 252..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..366
FT /note="Required for FFAT motif binding and phosphorylated
FT FFAT motif binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NHP6"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 363
FT /note="Required for phosphorylated FFAT motif binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NHP6"
FT SITE 374
FT /note="Required for FFAT motif binding"
FT /evidence="ECO:0000250|UniProtKB:Q8NHP6"
FT VAR_SEQ 160..164
FT /note="DMDFV -> VSILH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014047"
FT VAR_SEQ 165..518
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014048"
FT VAR_SEQ 474..486
FT /note="LNRLLESNRKLED -> FATSRCETDCSPH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014049"
FT VAR_SEQ 474..481
FT /note="LNRLLESN -> EESPLPSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014050"
FT VAR_SEQ 482..518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014051"
FT VAR_SEQ 487..518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014052"
FT VARIANT 288
FT /note="P -> S (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 249
FT /note="F -> S (in Ref. 1; BAB26972)"
FT /evidence="ECO:0000305"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:1WIC"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:1WIC"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:1WIC"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:1WIC"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:1WIC"
SQ SEQUENCE 518 AA; 59855 MW; 0AB04E38ACE46350 CRC64;
MAENNAQNKA KLISETRRRF EAEYVTEKSE KYDSRDVERL QQDDNWVESY LYWRHNVVDE
TLKMLDESFQ WRKEFSVNDL SESSIPRWLL ELGGIYLHGY DKEGNKLFWI RVKYHIKDQK
TIMDKKKLIA FWLERYAKRE NGKPITVMFD MSETGLNSID MDFVRFIINC FKVYYPKYLS
KIVIFDMPWI MNAAFKIVKS WLGPEAVSLL KFTSKNEIQE YVSVEYLPPH MGGTDPFKYS
YPPLVDDDFQ TPLCENGPIA SEDETSSKED IEGDGKETLE TISNEEPPAL SEKSNPTESV
SKKDENEKVD SKTKTFKKPL SVFKGPLLHI SPAEELYFGS IESGEKKTLI VLTNVTKNIV
AFKVRTTAPE KYRVKPSNSS CDPGASIDII VSPHGGLTVS AQDRFLIMAA EMEQSSGTGP
AELSQFWKEV PRNKVMEHRL RCHTVESSKP NSLMLKDSIS TMSDKTSEDL YLQLNRLLES
NRKLEDQLQR SIWFQQLLLA LTMVLLDFVV SFFYSLYN
//
