SLMAP_RABIT
ID SLMAP_RABIT Reviewed; 771 AA.
AC Q28623; Q28621; Q28622; Q9GK69;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Sarcolemmal membrane-associated protein;
DE Short=Sarcolemmal-associated protein;
GN Name=SLMAP; Synonyms=SLAP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9405447; DOI=10.1074/jbc.272.51.32384;
RA Wigle J.T., Demchyshyn L., Pratt M.A., Staines W.A., Salih M., Tuana B.S.;
RT "Molecular cloning, expression, and chromosomal assignment of sarcolemmal-
RT associated proteins. A family of acidic amphipathic alpha-helical proteins
RT associated with the membrane.";
RL J. Biol. Chem. 272:32384-32394(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
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 [3]
RP INTERACTION WITH MYOSIN.
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).
CC -!- FUNCTION: May play a role during myoblast fusion. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with myosin.
CC {ECO:0000250, ECO:0000269|PubMed:15591093}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:9405447}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:9405447}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Note=Membrane-associated.
CC Distributed in the transverse tubules and near the junctional
CC sarcoplasmic reticulum. Detected along the Z- and M-lines in
CC cardiomyocytes (By similarity). Localizes to the centrosomes in a
CC microtubule- dependent manner (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Some isoforms exhibit tissue specific expression.;
CC Name=1; Synonyms=Sarcolemmal-associated protein-3, SLAP3;
CC IsoId=Q28623-1; Sequence=Displayed;
CC Name=2; Synonyms=Sarcolemmal-associated protein-2, SLAP2;
CC IsoId=Q28623-2; Sequence=VSP_021521, VSP_021522;
CC Name=3; Synonyms=Sarcolemmal-associated protein-1, SLAP1;
CC IsoId=Q28623-3; Sequence=VSP_021519;
CC Name=4;
CC IsoId=Q28623-4; Sequence=VSP_021520, VSP_021523, VSP_021524;
CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level). Expressed in
CC heart, skeletal muscle, smooth muscle, kidney, spleen, pancreas and
CC brain. {ECO:0000269|PubMed:10986292, ECO:0000269|PubMed:9405447}.
CC -!- SIMILARITY: Belongs to the SLMAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65597.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U21155; AAA65598.1; -; mRNA.
DR EMBL; U21156; AAA65596.1; -; mRNA.
DR EMBL; U21157; AAA65597.1; ALT_INIT; mRNA.
DR EMBL; AF304449; AAG41948.1; -; mRNA.
DR RefSeq; XP_008258693.1; XM_008260471.2. [Q28623-1]
DR RefSeq; XP_017199132.1; XM_017343643.1. [Q28623-3]
DR AlphaFoldDB; Q28623; -.
DR SMR; Q28623; -.
DR Ensembl; ENSOCUT00000022997; ENSOCUP00000018690; ENSOCUG00000000827. [Q28623-1]
DR GeneID; 100009199; -.
DR CTD; 7871; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000157660; -.
DR InParanoid; Q28623; -.
DR OrthoDB; 902273at2759; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000000827; Expressed in aorta and 15 other tissues.
DR ExpressionAtlas; Q28623; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0006936; P:muscle contraction; IEA:InterPro.
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; 2.
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 Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..771
FT /note="Sarcolemmal membrane-associated protein"
FT /id="PRO_0000259664"
FT TOPO_DOM 1..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..771
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 /evidence="ECO:0000250"
FT REGION 420..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..202
FT /evidence="ECO:0000255"
FT COILED 230..381
FT /evidence="ECO:0000255"
FT COILED 452..742
FT /evidence="ECO:0000255"
FT COMPBIAS 420..447
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 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C219"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14BN4"
FT VAR_SEQ 1..449
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9405447"
FT /id="VSP_021519"
FT VAR_SEQ 1..408
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10986292"
FT /id="VSP_021520"
FT VAR_SEQ 1..348
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9405447"
FT /id="VSP_021521"
FT VAR_SEQ 380..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9405447"
FT /id="VSP_021522"
FT VAR_SEQ 409..466
FT /note="TKVVEETKLAKENQARAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNESLA
FT KVSLLK -> MDEQDLNESLAKVSLLKDDLQGAQSETEAKQEIQHLRKELIEAQELARA
FT SKQKCFELQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10986292"
FT /id="VSP_021523"
FT VAR_SEQ 742..771
FT /note="KPWPWMPMLAALVAVTAIVLYVPGLARASP -> PSILQPVPAVFIGLFLAF
FT LFWCFGPLW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10986292"
FT /id="VSP_021524"
SQ SEQUENCE 771 AA; 88525 MW; ED707B22628DD5DE CRC64;
MPSALAIFTC RPNSHPFQER HVYLDEPIKI GRSVARCRPA QNNATFDCKV LSRNHALVWF
DHKTGKFYLQ DTKSSNGTFI NSQRLSRGSE ESPPCEILSG DIIQFGVDVT ENTRKVTHGC
IVSTIKLFLP DGMEARLRSD VIHAPLPSPV DKVAANTPSM YSQELFQLSQ YLQEALHREQ
MLEQKLATLQ RLLAITQEAS DTSWQALIDE DRLLSRLEVM GNQLQACSKN QTEDSLRKEL
IALQEDKHNY ETTAKESLRR VLQEKIEVVR KLSEVERSLS NTEDECTHLK EMNERTQEEL
RELANKYNGA VNEIKDLSDK LKVAEGKQEE IQQKGQAEKK ELQHKIDEME EKEQELQAKI
EALQADNDFT NERLTALQEH LLSKSGGDCT FIHQFIECQK KLIVEGHLTK VVEETKLAKE
NQARAKESDL SDTLSPSKEK SSDDTTDAQM DEQDLNESLA KVSLLKALLE EERKAYRNQV
EESSKQIQVL QAQLQRLHMD IENLREEKDN EITSTRDELL SARDEILLLH QAAEKAASER
DTDIASLQEE LKKVRAELER WRKAASEYEK EVTSLQSSFQ LRCQQCEDQQ KEEATRLQGE
LEKLRKEWNV LETECHSLKK ENVLLSSELQ RQEKELHNSQ KQSLELTSDL SILQMTRKEL
ENQMGSLKEQ HLRDSADLKI LLSKAENQAK DVQKEYEKTQ TVLSELKLKF EMTEQEKQSI
TDELKQCKDN LKLLQEKGNN NKPWPWMPML AALVAVTAIV LYVPGLARAS P
