OPHN1_HUMAN
ID OPHN1_HUMAN Reviewed; 802 AA.
AC O60890; B9EIP8; Q5JQ81; Q6PCC1; Q8WX47;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Oligophrenin-1;
GN Name=OPHN1;
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 1), AND INVOLVEMENT IN MRXSBL.
RC TISSUE=Fetal brain;
RX PubMed=9582072; DOI=10.1038/31940;
RA Billuart P., Bienvenu T., Ronce N., des Portes V., Vinet M.C., Zemni R.,
RA Roest Crollius H., Carrie A., Fauchereau F., Cherry M., Brillaut S.,
RA Hamel B., Fryns J.-P., Beldjord C., Kahn A., Moraine C., Chelly J.;
RT "Oligophrenin-1 encodes a rhoGAP protein involved in X-linked mental
RT retardation.";
RL Nature 392:923-926(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN MRXSBL.
RX PubMed=10439959; DOI=10.1038/sj.ejhg.5200320;
RA Tentler D., Gustavsson P., Leisti J., Schueler M., Chelly J., Timonen E.,
RA Anneren G., Willard H.F., Dahl N.;
RT "Deletion including the oligophrenin-1 gene associated with enlarged
RT cerebral ventricles, cerebellar hypoplasia, seizures and ataxia.";
RL Eur. J. Hum. Genet. 7:541-548(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-45 AND MET-301.
RX PubMed=10818214; DOI=10.1016/s0003-3995(00)00015-0;
RA Billuart P., Chelly J., Carrie A., Vinet M.C., Couvert P., McDonell N.,
RA Zemni R., Kahn A., Moraine C., Beldjord C., Bienvenu T.;
RT "Determination of the gene structure of human oligophrenin-1 and
RT identification of three novel polymorphisms by screening of DNA from 164
RT patients with non-specific X-linked mental retardation.";
RL Ann. Genet. 43:5-9(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12777533; DOI=10.1093/molbev/msg134;
RA Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT chimpanzees.";
RL Mol. Biol. Evol. 20:1281-1289(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-39.
RC TISSUE=Lung, and Placenta;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [8]
RP VARIANT MRXSBL
RP GLU-PHE-SER-LEU-LEU-MET-ASN-GLY-LEU-LYS-ILE-PHE-ILE-LYS-CYS-LEU-199 INS.
RX PubMed=21796728; DOI=10.1002/humu.21567;
RA Pirozzi F., Di Raimo F.R., Zanni G., Bertini E., Billuart P.,
RA Tartaglione T., Tabolacci E., Brancaccio A., Neri G., Chiurazzi P.;
RT "Insertion of 16 amino acids in the BAR domain of the oligophrenin 1
RT protein causes mental retardation and cerebellar hypoplasia in an Italian
RT family.";
RL Hum. Mutat. 32:E2294-E2307(2011).
CC -!- FUNCTION: Stimulates GTP hydrolysis of members of the Rho family. Its
CC action on RHOA activity and signaling is implicated in growth and
CC stabilization of dendritic spines, and therefore in synaptic function.
CC Critical for the stabilization of AMPA receptors at postsynaptic sites.
CC Critical for the regulation of synaptic vesicle endocytosis at
CC presynaptic terminals. Required for the localization of NR1D1 to
CC dendrites, can suppress its repressor activity and protect it from
CC proteasomal degradation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HOMER1. Interacts with AMPA receptor complexes.
CC Interacts with SH3GL2 (endophilin-A1) (By similarity). Interacts (via
CC C-terminus) with NR1D1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynapse {ECO:0000250|UniProtKB:P0CAX5}.
CC Presynapse {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P0CAX5}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q99J31}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99J31}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60890-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60890-2; Sequence=VSP_055336, VSP_055337;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Billuart type (MRXSBL) [MIM:300486]: A disorder characterized by
CC significantly below average general intellectual functioning associated
CC with impairments in adaptive behavior and manifested during the
CC developmental period. MRXSBL patients manifest intellectual disability
CC associated with cerebellar hypoplasia and distinctive facial
CC dysmorphism. {ECO:0000269|PubMed:10439959, ECO:0000269|PubMed:21796728,
CC ECO:0000269|PubMed:9582072}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AJ001189; CAA04579.1; -; mRNA.
DR EMBL; AJ248245; CAB96181.1; -; Genomic_DNA.
DR EMBL; AJ248246; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248247; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248248; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248249; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248250; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248251; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248252; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248253; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248254; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248255; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248256; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248257; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248258; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248259; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248260; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248261; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248262; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248263; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248264; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248265; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248266; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AJ248267; CAB96181.1; JOINED; Genomic_DNA.
DR EMBL; AB102656; BAC81125.1; -; mRNA.
DR EMBL; AL157700; CAD18899.2; -; Genomic_DNA.
DR EMBL; AL158201; CAD18899.2; JOINED; Genomic_DNA.
DR EMBL; AL672138; CAD18899.2; JOINED; Genomic_DNA.
DR EMBL; Z82203; CAD18899.2; JOINED; Genomic_DNA.
DR EMBL; AL158201; CAI40982.1; -; Genomic_DNA.
DR EMBL; AL157700; CAI40982.1; JOINED; Genomic_DNA.
DR EMBL; AL672138; CAI40982.1; JOINED; Genomic_DNA.
DR EMBL; Z82203; CAI40982.1; JOINED; Genomic_DNA.
DR EMBL; AL672138; CAI41508.1; -; Genomic_DNA.
DR EMBL; AL157700; CAI41508.1; JOINED; Genomic_DNA.
DR EMBL; AL158201; CAI41508.1; JOINED; Genomic_DNA.
DR EMBL; Z82203; CAI41508.1; JOINED; Genomic_DNA.
DR EMBL; Z82203; CAI42695.1; -; Genomic_DNA.
DR EMBL; AL157700; CAI42695.1; JOINED; Genomic_DNA.
DR EMBL; AL158201; CAI42695.1; JOINED; Genomic_DNA.
DR EMBL; AL672138; CAI42695.1; JOINED; Genomic_DNA.
DR EMBL; BC059393; AAH59393.1; -; mRNA.
DR EMBL; BC140763; AAI40764.1; -; mRNA.
DR CCDS; CCDS14388.1; -. [O60890-1]
DR PIR; H59434; H59434.
DR RefSeq; NP_002538.1; NM_002547.2. [O60890-1]
DR RefSeq; XP_011529263.1; XM_011530961.1. [O60890-1]
DR AlphaFoldDB; O60890; -.
DR SMR; O60890; -.
DR BioGRID; 111029; 9.
DR IntAct; O60890; 2.
DR STRING; 9606.ENSP00000347710; -.
DR iPTMnet; O60890; -.
DR PhosphoSitePlus; O60890; -.
DR SwissPalm; O60890; -.
DR BioMuta; OPHN1; -.
DR EPD; O60890; -.
DR jPOST; O60890; -.
DR MassIVE; O60890; -.
DR MaxQB; O60890; -.
DR PaxDb; O60890; -.
DR PeptideAtlas; O60890; -.
DR PRIDE; O60890; -.
DR ProteomicsDB; 49656; -. [O60890-1]
DR Antibodypedia; 494; 115 antibodies from 24 providers.
DR DNASU; 4983; -.
DR Ensembl; ENST00000355520.6; ENSP00000347710.5; ENSG00000079482.14. [O60890-1]
DR GeneID; 4983; -.
DR KEGG; hsa:4983; -.
DR MANE-Select; ENST00000355520.6; ENSP00000347710.5; NM_002547.3; NP_002538.1.
DR UCSC; uc004dww.5; human. [O60890-1]
DR CTD; 4983; -.
DR DisGeNET; 4983; -.
DR GeneCards; OPHN1; -.
DR HGNC; HGNC:8148; OPHN1.
DR HPA; ENSG00000079482; Tissue enhanced (brain).
DR MalaCards; OPHN1; -.
DR MIM; 300127; gene.
DR MIM; 300486; phenotype.
DR neXtProt; NX_O60890; -.
DR OpenTargets; ENSG00000079482; -.
DR Orphanet; 137831; X-linked intellectual disability-cerebellar hypoplasia syndrome.
DR PharmGKB; PA31934; -.
DR VEuPathDB; HostDB:ENSG00000079482; -.
DR eggNOG; KOG1451; Eukaryota.
DR GeneTree; ENSGT00940000160157; -.
DR HOGENOM; CLU_011532_2_1_1; -.
DR InParanoid; O60890; -.
DR OMA; MKRMKQP; -.
DR OrthoDB; 693048at2759; -.
DR PhylomeDB; O60890; -.
DR TreeFam; TF316851; -.
DR PathwayCommons; O60890; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; O60890; -.
DR SIGNOR; O60890; -.
DR BioGRID-ORCS; 4983; 9 hits in 707 CRISPR screens.
DR ChiTaRS; OPHN1; human.
DR GeneWiki; OPHN1; -.
DR GenomeRNAi; 4983; -.
DR Pharos; O60890; Tbio.
DR PRO; PR:O60890; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O60890; protein.
DR Bgee; ENSG00000079482; Expressed in corpus callosum and 107 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; TAS:ProtInc.
DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:ARUK-UCL.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:ARUK-UCL.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IEA:Ensembl.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0030182; P:neuron differentiation; IMP:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; IMP:ARUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IMP:ARUK-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; TAS:ProtInc.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Disease variant;
KW Endocytosis; GTPase activation; Intellectual disability; Neurogenesis;
KW Reference proteome; Synapse.
FT CHAIN 1..802
FT /note="Oligophrenin-1"
FT /id="PRO_0000056760"
FT DOMAIN 265..368
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 380..564
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 569..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 278..311
FT /note="WALGISWVKYYCQYEKETKTLTMTPMEQKPGAKQ -> CVWGHRGIHWVSIS
FT QELLPLVGCEFWAPLLFIDP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055336"
FT VAR_SEQ 312..802
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055337"
FT VARIANT 39
FT /note="V -> I (in dbSNP:rs41303733)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_061184"
FT VARIANT 45
FT /note="A -> T (in dbSNP:rs148262378)"
FT /evidence="ECO:0000269|PubMed:10818214"
FT /id="VAR_013638"
FT VARIANT 199
FT /note="P -> PEFSLLMNGLKIFIKCL (in MRXSBL)"
FT /evidence="ECO:0000269|PubMed:21796728"
FT /id="VAR_066746"
FT VARIANT 301
FT /note="T -> M (in dbSNP:rs138108344)"
FT /evidence="ECO:0000269|PubMed:10818214"
FT /id="VAR_013639"
FT VARIANT 693
FT /note="M -> I (in dbSNP:rs36095561)"
FT /id="VAR_033452"
SQ SEQUENCE 802 AA; 91641 MW; A24D150048071608 CRC64;
MGHPPLEFSD CYLDSPDFRE RLKCYEQELE RTNKFIKDVI KDGNALISAM RNYSSAVQKF
SQTLQSFQFD FIGDTLTDDE INIAESFKEF AELLNEVENE RMMMVHNASD LLIKPLENFR
KEQIGFTKER KKKFEKDGER FYSLLDRHLH LSSKKKESQL QEADLQVDKE RHNFFESSLD
YVYQIQEVQE SKKFNIVEPV LAFLHSLFIS NSLTVELTQD FLPYKQQLQL SLQNTRNHFS
STREEMEELK KRMKEAPQTC KLPGQPTIEG YLYTQEKWAL GISWVKYYCQ YEKETKTLTM
TPMEQKPGAK QGPLDLTLKY CVRRKTESID KRFCFDIETN ERPGTITLQA LSEANRRLWM
EAMDGKEPIY HSPITKQQEM ELNEVGFKFV RKCINIIETK GIKTEGLYRT VGSNIQVQKL
LNAFFDPKCP GDVDFHNSDW DIKTITSSLK FYLRNLSEPV MTYRLHKELV SAAKSDNLDY
RLGAIHSLVY KLPEKNREML ELLIRHLVNV CEHSKENLMT PSNMGVIFGP TLMRAQEDTV
AAMMNIKFQN IVVEILIEHF GKIYLGPPEE SAAPPVPPPR VTARRHKPIT ISKRLLRERT
VFYTSSLDES EDEIQHQTPN GTITSSIEPP KPPQHPKLPI QRSGETDPGR KSPSRPILDG
KLEPCPEVDV GKLVSRLQDG GTKITPKATN GPMPGSGPTK TPSFHIKRPA PRPLAHHKEG
DADSFSKVRP PGEKPTIIRP PVRPPDPPCR AATPQKPEPK PDIVAGNAGE ITSSVVASRT
RFFETASRKT GSSQGRLPGD ES
