SLMAP_MOUSE
ID SLMAP_MOUSE Reviewed; 845 AA.
AC Q3URD3; Q3TLP0; Q3UIZ6; Q6ZPL8; Q8VC86; Q9EQ03;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sarcolemmal membrane-associated protein;
DE Short=Sarcolemmal-associated protein;
GN Name=Slmap; Synonyms=Kiaa1601, Slap;
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] (ISOFORM 4), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=10986292; DOI=10.1074/jbc.m007682200;
RA Wielowieyski P.A., Sevinc S., Guzzo R., Salih M., Wigle J.T., Tuana B.S.;
RT "Alternative splicing, expression, and genomic structure of the 3' region
RT of the gene encoding the sarcolemmal-associated proteins (SLAPs) defines a
RT novel class of coiled-coil tail-anchored membrane proteins.";
RL J. Biol. Chem. 275:38474-38481(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Fetal heart, Hippocampus, Lung, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [5]
RP PROTEIN SEQUENCE OF 744-759, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP INTERACTION WITH MYOSIN, HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=15591093; DOI=10.1152/ajpheart.01015.2004;
RA Guzzo R.M., Salih M., Moore E.D., Tuana B.S.;
RT "Molecular properties of cardiac tail-anchored membrane protein SLMAP are
RT consistent with structural role in arrangement of excitation-contraction
RT coupling apparatus.";
RL Am. J. Physiol. 288:H1810-H1819(2005).
RN [7]
RP FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15086317; DOI=10.1042/bj20031723;
RA Guzzo R.M., Wigle J., Salih M., Moore E.D., Tuana B.S.;
RT "Regulated expression and temporal induction of the tail-anchored
RT sarcolemmal-membrane-associated protein is critical for myoblast fusion.";
RL Biochem. J. 381:599-608(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=15126628; DOI=10.1242/jcs.01079;
RA Guzzo R.M., Sevinc S., Salih M., Tuana B.S.;
RT "A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a
RT component of the microtubule organizing centre.";
RL J. Cell Sci. 117:2271-2281(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, 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: May play a role during myoblast fusion.
CC {ECO:0000269|PubMed:15086317}.
CC -!- SUBUNIT: Homodimer. Interacts with myosin.
CC {ECO:0000269|PubMed:15591093}.
CC -!- INTERACTION:
CC Q3URD3-4; Q8BH43: Wasf2; NbExp=3; IntAct=EBI-3294998, EBI-643162;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Cytoplasm, myofibril,
CC sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line.
CC Note=Membrane-associated. Distributed in the transverse tubules and
CC near the junctional sarcoplasmic reticulum (By similarity). Detected
CC along the Z- and M-lines in cardiomyocytes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Localizes to the centrosomes in a
CC microtubule- dependent manner.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Localizes to the centrosomes in a
CC microtubule- dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q3URD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3URD3-2; Sequence=VSP_021517, VSP_021518;
CC Name=3;
CC IsoId=Q3URD3-3; Sequence=VSP_021514;
CC Name=4;
CC IsoId=Q3URD3-4; Sequence=VSP_021514, VSP_021518;
CC Name=5;
CC IsoId=Q3URD3-5; Sequence=VSP_021515, VSP_021516;
CC -!- TISSUE SPECIFICITY: Expressed in proliferating myoblasts and
CC differentiated myotubes (at protein level). Expressed in myoblasts,
CC cardiac and skeletal muscles. {ECO:0000269|PubMed:10986292,
CC ECO:0000269|PubMed:15086317}.
CC -!- DEVELOPMENTAL STAGE: Expressed in atrial and ventricular chambers of
CC the primitive heart at 9 dpc. Expressed in somites at 11 dpc. Expressed
CC in atrial and ventricular chambers and interventricular and interatrial
CC septum at 13 dpc. Expressed in myotubes between 13 and 15 dpc.
CC Expressed in skeletal muscles at 18 dpc. {ECO:0000269|PubMed:15086317}.
CC -!- SIMILARITY: Belongs to the SLMAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98213.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE24755.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF304451; AAG41950.1; -; mRNA.
DR EMBL; AK129403; BAC98213.1; ALT_INIT; mRNA.
DR EMBL; AK141597; BAE24755.1; ALT_INIT; mRNA.
DR EMBL; AK146685; BAE27359.1; -; mRNA.
DR EMBL; AK164911; BAE37961.1; -; mRNA.
DR EMBL; AK166396; BAE38752.1; -; mRNA.
DR EMBL; BC021457; AAH21457.1; -; mRNA.
DR CCDS; CCDS26880.1; -. [Q3URD3-2]
DR CCDS; CCDS79284.1; -. [Q3URD3-1]
DR RefSeq; NP_001297374.1; NM_001310445.1. [Q3URD3-1]
DR RefSeq; NP_001334423.1; NM_001347494.1.
DR RefSeq; NP_114397.3; NM_032008.4. [Q3URD3-2]
DR RefSeq; XP_017171716.1; XM_017316227.1.
DR RefSeq; XP_017171717.1; XM_017316228.1.
DR AlphaFoldDB; Q3URD3; -.
DR SMR; Q3URD3; -.
DR BioGRID; 219996; 26.
DR IntAct; Q3URD3; 2.
DR STRING; 10090.ENSMUSP00000117816; -.
DR iPTMnet; Q3URD3; -.
DR PhosphoSitePlus; Q3URD3; -.
DR EPD; Q3URD3; -.
DR MaxQB; Q3URD3; -.
DR PaxDb; Q3URD3; -.
DR PeptideAtlas; Q3URD3; -.
DR PRIDE; Q3URD3; -.
DR ProteomicsDB; 261422; -. [Q3URD3-1]
DR ProteomicsDB; 261423; -. [Q3URD3-2]
DR ProteomicsDB; 261424; -. [Q3URD3-3]
DR ProteomicsDB; 261425; -. [Q3URD3-4]
DR ProteomicsDB; 261426; -. [Q3URD3-5]
DR Antibodypedia; 1193; 72 antibodies from 18 providers.
DR DNASU; 83997; -.
DR Ensembl; ENSMUST00000038522; ENSMUSP00000046956; ENSMUSG00000021870. [Q3URD3-2]
DR Ensembl; ENSMUST00000102956; ENSMUSP00000100021; ENSMUSG00000021870. [Q3URD3-2]
DR Ensembl; ENSMUST00000139075; ENSMUSP00000117816; ENSMUSG00000021870. [Q3URD3-1]
DR GeneID; 83997; -.
DR KEGG; mmu:83997; -.
DR UCSC; uc007ssq.1; mouse. [Q3URD3-5]
DR UCSC; uc007ssr.1; mouse. [Q3URD3-2]
DR UCSC; uc007sss.1; mouse. [Q3URD3-1]
DR CTD; 7871; -.
DR MGI; MGI:1933549; Slmap.
DR VEuPathDB; HostDB:ENSMUSG00000021870; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000157660; -.
DR HOGENOM; CLU_359254_0_0_1; -.
DR InParanoid; Q3URD3; -.
DR OMA; XVIHAPL; -.
DR OrthoDB; 902273at2759; -.
DR PhylomeDB; Q3URD3; -.
DR TreeFam; TF318787; -.
DR BioGRID-ORCS; 83997; 7 hits in 76 CRISPR screens.
DR ChiTaRS; Slmap; mouse.
DR PRO; PR:Q3URD3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3URD3; protein.
DR Bgee; ENSMUSG00000021870; Expressed in aorta tunica media and 252 other tissues.
DR ExpressionAtlas; Q3URD3; baseline and differential.
DR Genevisible; Q3URD3; MM.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; ISO:MGI.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001363; Prot_inh_fetuin_CS.
DR InterPro; IPR030498; SLMAP.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR15715:SF22; PTHR15715:SF22; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..845
FT /note="Sarcolemmal membrane-associated protein"
FT /id="PRO_0000259663"
FT TOPO_DOM 1..819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..845
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 28..85
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..163
FT /note="Necessary for targeting to centrosomes"
FT REGION 451..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..202
FT /evidence="ECO:0000255"
FT COILED 231..388
FT /evidence="ECO:0000255"
FT COILED 506..816
FT /evidence="ECO:0000255"
FT COMPBIAS 451..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14BN4"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C219"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14BN4"
FT VAR_SEQ 1..483
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10986292,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021514"
FT VAR_SEQ 1..348
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021515"
FT VAR_SEQ 396..434
FT /note="GIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFLECQK -> E (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021516"
FT VAR_SEQ 414..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_021517"
FT VAR_SEQ 816..845
FT /note="KPWPWMPMLAALVAVTAMVLYVPGLARASP -> PSILQPVPAVFIGLFLAF
FT LFWCFGPLW (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10986292,
FT ECO:0000303|PubMed:14621295"
FT /id="VSP_021518"
FT CONFLICT 682
FT /note="E -> G (in Ref. 1; AAG41950)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..697
FT /note="EN -> GD (in Ref. 1; AAG41950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 845 AA; 96933 MW; FC73049C382CA17F CRC64;
MPSALAIFTC RPNSHPFQER HVYLDEPIKI GRSVARCRPA QNNATFDCKV LSRNHALVWF
DHKTSKFYLQ DTKSSNGTFI NSQRLSRGSE ESPPCEILSG DIIQFGVDVT ENTRKVTHGC
IVSTIKLFLP DGMEARLRSD VIHAPLPSPV DKVAANTPSM YSQELFQLSQ YLQEALHREQ
MLEQKLATLQ RLLAITQEAS DTSWQALIDE DRLLSRLEVM GNQLQACSKN QTEDSLRKEL
IALQEDKHSY ETTAKESLRR VLQEKIEVVR KLSEVERSLS NTEDECTHLK EMNERTQEEL
RELANKYNGA VNEIKDLSDK LKVAEGKQEE IQQKGQAEKK ELQTKIDEME EKEQELQAKI
EALQADNDFT NERLTALQVR LEHLQEKTLK ECSSLGIQVD DFLPKINGST EKEHLLSKSG
GDCTFIHQFL ECQKKLMVQG HLTKVVEESK LSKENQAKAK ESDLSDTLSP SKEKSSDDTT
DAQMDEQDLN EPLAKVSLLK DDLQGTQSET EAKQDIQHLR KELVEAQELA RTSKQKCFEL
QALLEEERKA YRNQVEESAK QIQVLQVQLQ KLHMDMENLQ EEKDTEISST RDKLLSAQDE
ILLLRQAAAE AVSERDTDFV SLQEELKKVR AELEGWRKAA SEYENEIRSL QSSFQLRCQQ
CEDQQREEAT RLQGELEKLK KEWDVLETEC HSLKKENVLL SSELQRQEKE LHNSQKQSFE
LTSDLSILQM TRKELEKQVG SLKEQHLRDA ADLKTLLSKA ENQAKDVQKE YEKTQTVLSE
LKLKFEMTEQ EKQSITDELK QCKDNLKLLR EKGNNKPWPW MPMLAALVAV TAMVLYVPGL
ARASP
