SLMAP_HUMAN
ID SLMAP_HUMAN Reviewed; 828 AA.
AC Q14BN4; Q14C95; Q6AI54; Q6UXC9; Q6ZVQ8; Q8NCW9; Q9H297; Q9HCH1; Q9Y681;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sarcolemmal membrane-associated protein;
DE Short=Sarcolemmal-associated protein;
GN Name=SLMAP; Synonyms=KIAA1601, SLAP; ORFNames=UNQ1847/PRO3577;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 528-828.
RC TISSUE=Fetal liver, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-828 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May play a role during myoblast fusion. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with myosin (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q14BN4; Q13188: STK3; NbExp=7; IntAct=EBI-1043216, EBI-992580;
CC Q14BN4; Q13043: STK4; NbExp=7; IntAct=EBI-1043216, EBI-367376;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Note=Membrane-
CC associated. Distributed in the transverse tubules and near the
CC junctional sarcoplasmic reticulum. Detected along the Z- and M-lines in
CC cardiomyocytes. Centrosome. Localizes to the centrosomes in a
CC microtubule- dependent manner (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q14BN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14BN4-2; Sequence=VSP_021502;
CC Name=3;
CC IsoId=Q14BN4-3; Sequence=VSP_021503;
CC Name=4;
CC IsoId=Q14BN4-4; Sequence=VSP_021500, VSP_021501, VSP_021512;
CC Name=5;
CC IsoId=Q14BN4-5; Sequence=VSP_021499, VSP_021513;
CC Name=6;
CC IsoId=Q14BN4-6; Sequence=VSP_021505, VSP_021508, VSP_021509;
CC Name=7;
CC IsoId=Q14BN4-7; Sequence=VSP_021504, VSP_021506;
CC Name=8;
CC IsoId=Q14BN4-8; Sequence=VSP_021499, VSP_021507, VSP_021510,
CC VSP_021511;
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SLMAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH10369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF304450; AAG41949.1; -; mRNA.
DR EMBL; AF100750; AAD43014.1; -; mRNA.
DR EMBL; AY358410; AAQ88776.1; ALT_INIT; mRNA.
DR EMBL; AK124200; BAC85803.1; -; mRNA.
DR EMBL; AL834538; CAD39194.1; -; mRNA.
DR EMBL; CR627321; CAH10369.1; ALT_INIT; mRNA.
DR EMBL; BC114627; AAI14628.1; -; mRNA.
DR EMBL; BC115701; AAI15702.1; -; mRNA.
DR EMBL; AB046821; BAB13427.1; -; mRNA.
DR CCDS; CCDS33774.1; -. [Q14BN4-3]
DR CCDS; CCDS77757.1; -. [Q14BN4-1]
DR CCDS; CCDS77758.1; -. [Q14BN4-2]
DR RefSeq; NP_001291349.1; NM_001304420.2. [Q14BN4-1]
DR RefSeq; NP_001291350.1; NM_001304421.2. [Q14BN4-2]
DR RefSeq; NP_001298107.1; NM_001311178.1. [Q14BN4-5]
DR RefSeq; NP_001298108.1; NM_001311179.1. [Q14BN4-8]
DR RefSeq; NP_009090.2; NM_007159.4. [Q14BN4-3]
DR RefSeq; XP_005265518.1; XM_005265461.3.
DR RefSeq; XP_005265523.1; XM_005265466.3.
DR RefSeq; XP_005265528.1; XM_005265471.3.
DR RefSeq; XP_016862659.1; XM_017007170.1. [Q14BN4-5]
DR PDB; 6AKM; X-ray; 2.30 A; B=167-226.
DR PDB; 6AR0; X-ray; 1.08 A; A=1-140.
DR PDB; 6AR2; X-ray; 1.55 A; A/B=1-140.
DR PDBsum; 6AKM; -.
DR PDBsum; 6AR0; -.
DR PDBsum; 6AR2; -.
DR AlphaFoldDB; Q14BN4; -.
DR SMR; Q14BN4; -.
DR BioGRID; 113620; 113.
DR IntAct; Q14BN4; 73.
DR MINT; Q14BN4; -.
DR STRING; 9606.ENSP00000295951; -.
DR iPTMnet; Q14BN4; -.
DR PhosphoSitePlus; Q14BN4; -.
DR BioMuta; SLMAP; -.
DR DMDM; 118597508; -.
DR EPD; Q14BN4; -.
DR jPOST; Q14BN4; -.
DR MassIVE; Q14BN4; -.
DR MaxQB; Q14BN4; -.
DR PaxDb; Q14BN4; -.
DR PeptideAtlas; Q14BN4; -.
DR PRIDE; Q14BN4; -.
DR ProteomicsDB; 60298; -. [Q14BN4-1]
DR ProteomicsDB; 60299; -. [Q14BN4-2]
DR ProteomicsDB; 60300; -. [Q14BN4-3]
DR ProteomicsDB; 60301; -. [Q14BN4-4]
DR ProteomicsDB; 60302; -. [Q14BN4-5]
DR ProteomicsDB; 60303; -. [Q14BN4-6]
DR ProteomicsDB; 60304; -. [Q14BN4-7]
DR ProteomicsDB; 60305; -. [Q14BN4-8]
DR Antibodypedia; 1193; 72 antibodies from 18 providers.
DR DNASU; 7871; -.
DR Ensembl; ENST00000295951.7; ENSP00000295951.3; ENSG00000163681.16. [Q14BN4-3]
DR Ensembl; ENST00000295952.7; ENSP00000295952.3; ENSG00000163681.16. [Q14BN4-3]
DR Ensembl; ENST00000383718.7; ENSP00000373224.3; ENSG00000163681.16. [Q14BN4-6]
DR Ensembl; ENST00000449503.6; ENSP00000412945.2; ENSG00000163681.16. [Q14BN4-2]
DR Ensembl; ENST00000494088.6; ENSP00000418218.2; ENSG00000163681.16. [Q14BN4-5]
DR Ensembl; ENST00000659705.1; ENSP00000499241.1; ENSG00000163681.16. [Q14BN4-1]
DR GeneID; 7871; -.
DR KEGG; hsa:7871; -.
DR UCSC; uc003djc.2; human. [Q14BN4-1]
DR CTD; 7871; -.
DR DisGeNET; 7871; -.
DR GeneCards; SLMAP; -.
DR GeneReviews; SLMAP; -.
DR HGNC; HGNC:16643; SLMAP.
DR HPA; ENSG00000163681; Low tissue specificity.
DR MalaCards; SLMAP; -.
DR MIM; 602701; gene.
DR neXtProt; NX_Q14BN4; -.
DR OpenTargets; ENSG00000163681; -.
DR Orphanet; 130; Brugada syndrome.
DR PharmGKB; PA38179; -.
DR VEuPathDB; HostDB:ENSG00000163681; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000157660; -.
DR HOGENOM; CLU_041551_0_1_1; -.
DR InParanoid; Q14BN4; -.
DR OrthoDB; 902273at2759; -.
DR PhylomeDB; Q14BN4; -.
DR TreeFam; TF318787; -.
DR PathwayCommons; Q14BN4; -.
DR SignaLink; Q14BN4; -.
DR BioGRID-ORCS; 7871; 62 hits in 1078 CRISPR screens.
DR ChiTaRS; SLMAP; human.
DR GeneWiki; SLMAP; -.
DR GenomeRNAi; 7871; -.
DR Pharos; Q14BN4; Tbio.
DR PRO; PR:Q14BN4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14BN4; protein.
DR Bgee; ENSG00000163681; Expressed in saphenous vein and 189 other tissues.
DR ExpressionAtlas; Q14BN4; baseline and differential.
DR Genevisible; Q14BN4; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IMP:BHF-UCL.
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 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..828
FT /note="Sarcolemmal membrane-associated protein"
FT /id="PRO_0000259662"
FT TOPO_DOM 1..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..828
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 433..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..202
FT /evidence="ECO:0000255"
FT COILED 230..388
FT /evidence="ECO:0000255"
FT COILED 477..799
FT /evidence="ECO:0000255"
FT COMPBIAS 433..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C219"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..466
FT /note="Missing (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10986292,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_021499"
FT VAR_SEQ 1..348
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_021500"
FT VAR_SEQ 379..436
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_021501"
FT VAR_SEQ 379..417
FT /note="VRLEHLQEKTLKECSSLEHLLSKSGGDCTFIHQFIECQK -> E (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021502"
FT VAR_SEQ 379..395
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_021503"
FT VAR_SEQ 396..428
FT /note="EHLLSKSGGDCTFIHQFIECQKKLIVEGHLTKA -> ADRRRASNQSGRRNK
FT AFKRFVFCFSMFFDSSFG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_021504"
FT VAR_SEQ 396..417
FT /note="EHLLSKSGGDCTFIHQFIECQK -> GIQVDDFLPKINGSTEKE (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021505"
FT VAR_SEQ 429..828
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_021506"
FT VAR_SEQ 484..524
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021507"
FT VAR_SEQ 484..510
FT /note="DDLQGAQSEIEAKQEIQHLRKELIEAQ -> GTLTCFYDIVNQGIKSPFAIK
FT SVLDIM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021508"
FT VAR_SEQ 511..828
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021509"
FT VAR_SEQ 754..778
FT /note="YEKTQTVLSELKLKFEMTEQEKQSI -> VKRKDIMSPIMVGLKAKSKSDIH
FT AS (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021510"
FT VAR_SEQ 779..828
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021511"
FT VAR_SEQ 798
FT /note="N -> NPSILQPVPARIHRPIPGFPDMVIRSIVERK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_021512"
FT VAR_SEQ 799..828
FT /note="KPWPWMPMLAALVAVTAIVLYVPGLARASP -> PSILQPVPAVFIGLFLAF
FT LFWCFGPLW (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10986292"
FT /id="VSP_021513"
FT CONFLICT 493
FT /note="I -> T (in Ref. 1; AAG41949)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="T -> A (in Ref. 1; AAG41949)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="A -> Q (in Ref. 2; AAD43014)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6AR0"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6AR2"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6AR0"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6AR2"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6AR0"
FT HELIX 167..199
FT /evidence="ECO:0007829|PDB:6AKM"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6AKM"
SQ SEQUENCE 828 AA; 95198 MW; 20F5FA38174CA383 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 NERLTALQVR LEHLQEKTLK ECSSLEHLLS KSGGDCTFIH QFIECQKKLI
VEGHLTKAVE ETKLSKENQT RAKESDFSDT LSPSKEKSSD DTTDAQMDEQ DLNEPLAKVS
LLKDDLQGAQ SEIEAKQEIQ HLRKELIEAQ ELARTSKQKC FELQALLEEE RKAYRNQVEE
STKQIQVLQA QLQRLHIDTE NLREEKDSEI TSTRDELLSA RDEILLLHQA AAKVASERDT
DIASLQEELK KVRAELERWR KAASEYEKEI TSLQNSFQLR CQQCEDQQRE EATRLQGELE
KLRKEWNALE TECHSLKREN VLLSSELQRQ EKELHNSQKQ SLELTSDLSI LQMSRKELEN
QVGSLKEQHL RDSADLKTLL SKAENQAKDV QKEYEKTQTV LSELKLKFEM TEQEKQSITD
ELKQCKNNLK LLREKGNNKP WPWMPMLAAL VAVTAIVLYV PGLARASP
