SLMAP_RAT
ID SLMAP_RAT Reviewed; 858 AA.
AC P0C219;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sarcolemmal membrane-associated protein;
GN Name=Slmap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472 AND SER-476, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role during myoblast fusion. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with myosin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:15591093}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:15591093}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Note=Distributed in the
CC transverse tubules and near the junctional sarcoplasmic reticulum.
CC Detected along the Z-lines and M-lines in cardiomyocytes. Membrane-
CC associated (By similarity). Localizes to the centrosomes in a
CC microtubule- dependent manner (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLMAP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03100912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03100133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03100672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03100596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C219; -.
DR SMR; P0C219; -.
DR iPTMnet; P0C219; -.
DR PhosphoSitePlus; P0C219; -.
DR PRIDE; P0C219; -.
DR UCSC; RGD:1307674; rat.
DR RGD; 1307674; Slmap.
DR InParanoid; P0C219; -.
DR PhylomeDB; P0C219; -.
DR PRO; PR:P0C219; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; ISO:RGD.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
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 Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..858
FT /note="Sarcolemmal membrane-associated protein"
FT /id="PRO_0000259665"
FT TOPO_DOM 1..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 28..85
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..165
FT /note="Necessary for targeting to centrosomes"
FT /evidence="ECO:0000250"
FT REGION 456..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..204
FT /evidence="ECO:0000255"
FT COILED 232..381
FT /evidence="ECO:0000255"
FT COILED 516..829
FT /evidence="ECO:0000255"
FT COMPBIAS 456..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14BN4"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 858 AA; 98224 MW; 9BDAF795710C2FC9 CRC64;
MPSALAIFTC RPNSHPFQER HVYLDEPIKI GRSVARCRPA QNNATFDCKV LSRNHALVWF
DHKTSKFYLQ DTKSSNGTFI NSQRLSRGSE ESPPCEILSG DIIQFGVDVT ENTRKVVTHG
CIVSTIKLFL PDGMEARLRS DDVIHAPLPS PVDKVAANTP SMYSQELFQL SQYLQEALHR
EQMLEQKLAT LQRLLAITQE ASDTSWQALI DEDRLLSRLE VMGNQLQACS KNQTEDSLRK
ELVALQEDKH SYETTAKESL RRVLQEKIEV VRKLSEVERS LSNTEDECTH LREMNERTQE
ELRELANKYN GAVNEIKDLS DKLKAAEGKQ EEIQQKGQAE KKELQAKIDD MEEKEQELQA
KIEALQADND FTNERLTALQ VVRLEPLQEK TLKECSSLGG IQVDDFLPKI NGSTEKEERL
LSKSGGDCTF IHQFIECQKK KLMVQGHLTK VVEESKLSKE ENQAKAKESD LSDTLSPSKE
KSSDDTTDDA QMDEQDLNEP LAKVSLLKDD DLQGTQAETE AKQDTQHLRK ELVEAQELAR
ASKQKCFDLQ AALLEEERKA YRNQVEESAK QIQVLQVVQL QRLHMDMENL QEEKDTEISS
TRDKLLSAQD EILLLHQAAA KAVSERDTDF MSLQEELKKV RAELEGWRKA ASEYEEEIRS
LQSTFQLRCQ QCEVQQREEA TRLQGGELEK LKKEWDVLEN ECRSLKKENV LLSSELQRQE
KELHNNSQKQ SLELTSDLSI LQMTRKELEN QMGSLKEQHL RDEADLKTLL SKAENQAKDV
QKEYEKTQTV LSELKLKFEM TEQEKQSITD ELKQCKDNLK LLREKGNNKP WPWMPMVAAL
VAVTAMVLYV PGLARASP
