MYRIP_HUMAN
ID MYRIP_HUMAN Reviewed; 859 AA.
AC Q8NFW9; B3KWM3; B3KWW4; B7Z2H1; B7Z9V3; G3XAI8; Q32M41; Q32M42; Q569F7;
AC Q8IUF5; Q9Y3V4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Rab effector MyRIP;
DE AltName: Full=Exophilin-8;
DE AltName: Full=Myosin-VIIa- and Rab-interacting protein;
DE AltName: Full=Synaptotagmin-like protein lacking C2 domains C;
DE Short=SlaC2-c;
DE Short=Slp homolog lacking C2 domains c;
GN Name=MYRIP; Synonyms=SLAC2C;
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), INTERACTION WITH RAB27A AND MYO7A,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=11964381; DOI=10.1093/embo-reports/kvf090;
RA El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S., Desnos C.,
RA Henry J.-P., Wolfrum U., Darchen F., Petit C.;
RT "MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal
RT melanosomes.";
RL EMBO Rep. 3:463-470(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MYO5A AND
RP MYO7A.
RX PubMed=12221080; DOI=10.1074/jbc.m203862200;
RA Fukuda M., Kuroda T.S.;
RT "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a
RT novel linker protein that interacts with Rab27, myosin Va/VIIa, and
RT actin.";
RL J. Biol. Chem. 277:43096-43103(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain, Hippocampus, Teratocarcinoma, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND VARIANT
RP THR-312.
RC TISSUE=Lymph;
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 699-859.
RC TISSUE=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 [8]
RP INTERACTION WITH PRKAR2A.
RX PubMed=17827149; DOI=10.1074/jbc.m705167200;
RA Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.;
RT "MyRIP anchors protein kinase A to the exocyst complex.";
RL J. Biol. Chem. 282:33155-33167(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Rab effector protein involved in melanosome transport. Serves
CC as link between melanosome-bound RAB27A and the motor proteins MYO5A
CC and MYO7A. May link RAB27A-containing vesicles to actin filaments.
CC Functions as a protein kinase A-anchoring protein (AKAP). May act as a
CC scaffolding protein that links PKA to components of the exocytosis
CC machinery, thus facilitating exocytosis, including insulin release (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds MYO5A, MYO7A and F-actin (By similarity). Binds RAB27A
CC that has been activated by GTP-binding via its N-terminus. Interacts
CC with PRKAR2A. Interacts with components of the exocyst complex,
CC including EXOC3 and EXOC4 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NFW9; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-1759414, EBI-747505;
CC Q8NFW9; O43482: OIP5; NbExp=3; IntAct=EBI-1759414, EBI-536879;
CC Q8NFW9; P51159: RAB27A; NbExp=3; IntAct=EBI-1759414, EBI-716881;
CC Q8NFW9; O00194: RAB27B; NbExp=3; IntAct=EBI-1759414, EBI-10179046;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}.
CC Note=In presynaptic and postsynaptic areas in photoreceptor cells and
CC in the basal microvilli of retinal pigment epithelium cells. Associated
CC with melanosomes. Colocalizes with actin filaments.
CC {ECO:0000250|UniProtKB:Q7TNY7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8NFW9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFW9-2; Sequence=VSP_043541;
CC Name=3;
CC IsoId=Q8NFW9-3; Sequence=VSP_043540;
CC Name=4;
CC IsoId=Q8NFW9-4; Sequence=VSP_043539;
CC Name=5;
CC IsoId=Q8NFW9-5; Sequence=VSP_043542, VSP_043543;
CC Name=6;
CC IsoId=Q8NFW9-6; Sequence=VSP_054896, VSP_054897;
CC -!- TISSUE SPECIFICITY: Detected in brain, skin, heart, adrenal medulla,
CC pancreas, intestine, liver, kidney, muscle and testis.
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DR EMBL; AF396687; AAM43954.1; -; mRNA.
DR EMBL; AB083783; BAC15555.1; -; mRNA.
DR EMBL; AK125334; BAG54185.1; -; mRNA.
DR EMBL; AK126013; BAG54276.1; -; mRNA.
DR EMBL; AK294714; BAH11857.1; -; mRNA.
DR EMBL; AK316068; BAH14439.1; -; mRNA.
DR EMBL; AC099331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64595.1; -; Genomic_DNA.
DR EMBL; BC092512; AAH92512.1; -; mRNA.
DR EMBL; BC109311; AAI09312.1; -; mRNA.
DR EMBL; BC109312; AAI09313.1; -; mRNA.
DR EMBL; AL050090; CAB43262.1; -; mRNA.
DR CCDS; CCDS2689.1; -. [Q8NFW9-1]
DR CCDS; CCDS68390.1; -. [Q8NFW9-2]
DR CCDS; CCDS68391.1; -. [Q8NFW9-6]
DR CCDS; CCDS68392.1; -. [Q8NFW9-4]
DR PIR; T08739; T08739.
DR RefSeq; NP_001271352.1; NM_001284423.1. [Q8NFW9-1]
DR RefSeq; NP_001271353.1; NM_001284424.1. [Q8NFW9-2]
DR RefSeq; NP_001271354.1; NM_001284425.1. [Q8NFW9-6]
DR RefSeq; NP_001271355.1; NM_001284426.1. [Q8NFW9-4]
DR RefSeq; NP_056275.2; NM_015460.3. [Q8NFW9-1]
DR RefSeq; XP_011531877.1; XM_011533575.1. [Q8NFW9-1]
DR AlphaFoldDB; Q8NFW9; -.
DR SMR; Q8NFW9; -.
DR BioGRID; 117424; 5.
DR DIP; DIP-48949N; -.
DR IntAct; Q8NFW9; 9.
DR MINT; Q8NFW9; -.
DR STRING; 9606.ENSP00000301972; -.
DR GlyGen; Q8NFW9; 8 sites, 1 O-linked glycan (8 sites).
DR iPTMnet; Q8NFW9; -.
DR PhosphoSitePlus; Q8NFW9; -.
DR BioMuta; MYRIP; -.
DR DMDM; 116242669; -.
DR jPOST; Q8NFW9; -.
DR MassIVE; Q8NFW9; -.
DR PaxDb; Q8NFW9; -.
DR PeptideAtlas; Q8NFW9; -.
DR PRIDE; Q8NFW9; -.
DR ProteomicsDB; 61588; -.
DR ProteomicsDB; 73377; -. [Q8NFW9-1]
DR ProteomicsDB; 73378; -. [Q8NFW9-2]
DR ProteomicsDB; 73379; -. [Q8NFW9-3]
DR ProteomicsDB; 73380; -. [Q8NFW9-4]
DR ProteomicsDB; 73381; -. [Q8NFW9-5]
DR Antibodypedia; 28983; 175 antibodies from 27 providers.
DR DNASU; 25924; -.
DR Ensembl; ENST00000302541.11; ENSP00000301972.6; ENSG00000170011.14. [Q8NFW9-1]
DR Ensembl; ENST00000396217.7; ENSP00000379519.3; ENSG00000170011.14. [Q8NFW9-6]
DR Ensembl; ENST00000425621.5; ENSP00000389323.1; ENSG00000170011.14. [Q8NFW9-2]
DR Ensembl; ENST00000444716.5; ENSP00000398665.1; ENSG00000170011.14. [Q8NFW9-1]
DR Ensembl; ENST00000458292.5; ENSP00000413392.1; ENSG00000170011.14. [Q8NFW9-5]
DR Ensembl; ENST00000539167.2; ENSP00000438297.1; ENSG00000170011.14. [Q8NFW9-4]
DR GeneID; 25924; -.
DR KEGG; hsa:25924; -.
DR MANE-Select; ENST00000302541.11; ENSP00000301972.6; NM_015460.4; NP_056275.2.
DR UCSC; uc003cka.5; human. [Q8NFW9-1]
DR CTD; 25924; -.
DR DisGeNET; 25924; -.
DR GeneCards; MYRIP; -.
DR HGNC; HGNC:19156; MYRIP.
DR HPA; ENSG00000170011; Tissue enhanced (brain).
DR MIM; 611790; gene.
DR neXtProt; NX_Q8NFW9; -.
DR OpenTargets; ENSG00000170011; -.
DR PharmGKB; PA38800; -.
DR VEuPathDB; HostDB:ENSG00000170011; -.
DR eggNOG; ENOG502QPUS; Eukaryota.
DR GeneTree; ENSGT00950000183138; -.
DR HOGENOM; CLU_008568_0_0_1; -.
DR InParanoid; Q8NFW9; -.
DR OMA; DNGQCIQ; -.
DR OrthoDB; 492485at2759; -.
DR PhylomeDB; Q8NFW9; -.
DR TreeFam; TF331599; -.
DR PathwayCommons; Q8NFW9; -.
DR Reactome; R-HSA-264876; Insulin processing.
DR SignaLink; Q8NFW9; -.
DR BioGRID-ORCS; 25924; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; MYRIP; human.
DR GenomeRNAi; 25924; -.
DR Pharos; Q8NFW9; Tbio.
DR PRO; PR:Q8NFW9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NFW9; protein.
DR Bgee; ENSG00000170011; Expressed in pigmented layer of retina and 178 other tissues.
DR ExpressionAtlas; Q8NFW9; baseline and differential.
DR Genevisible; Q8NFW9; HS.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; ISS:UniProtKB.
DR GO; GO:0000145; C:exocyst; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR006788; Myrip/Melanophilin.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF04698; Rab_eff_C; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..859
FT /note="Rab effector MyRIP"
FT /id="PRO_0000190224"
FT DOMAIN 4..124
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT ZN_FING 63..105
FT /note="FYVE-type"
FT REGION 143..560
FT /note="Myosin-binding"
FT REGION 193..209
FT /note="PKA-binding"
FT /evidence="ECO:0000250"
FT REGION 232..248
FT /note="Negative regulation of PKA-binding"
FT /evidence="ECO:0000250"
FT REGION 251..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..856
FT /note="Actin-binding"
FT REGION 783..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3I4"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TNY7"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043539"
FT VAR_SEQ 1..112
FT /note="MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEERLSELKQKLDEEGSKCSI
FT LSKHQQFVEHCCMRCCSPFTFLVNTKRQCGDCKFNVCKSCCSYQKHEKAWVCCVCQQAR
FT L -> MQKSLRPIGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043540"
FT VAR_SEQ 1..67
FT /note="MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEERLSELKQKLDEEGSKCSI
FT LSKHQQFVEHCCMRC -> MRKAASAASSRSTSSLWSTAACAAARPSPSSSTPSASVEI
FT ANSMSARAAAPTRSTKRPGSAASASKR (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054896"
FT VAR_SEQ 68..156
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054897"
FT VAR_SEQ 636..700
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043541"
FT VAR_SEQ 637
FT /note="F -> S (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043542"
FT VAR_SEQ 638..859
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043543"
FT VARIANT 312
FT /note="A -> T (in dbSNP:rs59923220)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_061755"
FT VARIANT 365
FT /note="P -> L (in dbSNP:rs55785561)"
FT /id="VAR_061756"
FT VARIANT 673
FT /note="P -> S (in dbSNP:rs34800524)"
FT /id="VAR_051717"
FT CONFLICT 130
FT /note="K -> E (in Ref. 3; BAG54185)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="R -> G (in Ref. 3; BAG54276)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="E -> G (in Ref. 3; BAG54276)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="D -> E (in Ref. 1; AAM43954)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="A -> T (in Ref. 3; BAH14439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 95706 MW; C1087932C405DFDD CRC64;
MGRKLDLSGL TDDETEHVLQ VVQRDFNLRK KEEERLSELK QKLDEEGSKC SILSKHQQFV
EHCCMRCCSP FTFLVNTKRQ CGDCKFNVCK SCCSYQKHEK AWVCCVCQQA RLLRAQSLEW
FYNNVKSRFK RFGSAKVLKN LYRKHRLESG ACFDILGGSL FESNLENEGS ISGSDSTFYR
QSEGHSVMDT LAVALRVAEE AIEEAISKAE AYGDSLDKQN EASYLRDHKE ELTEELATTI
LQKIIRKQKS KSEQQVEEEP GWPHPQSCST KVADEGTSAS PGGYRAPAAL WRSQSAFSIT
GEEALKTPPV EAPSRQPRDQ GQHPRAESAL PSWKSVDRLD ETNLAPVLQS PDGNWVALKD
GAPPPTRLLA KPKSGTFQAL EVASSVASAY DEMGSDSEED FDWSEALSKL CPRSRALPRN
PQPQPTQAQS SDQGPIAASP SSALSPNPEA MCSDSETSSA GSSREVGHQA RLSWLQRKAP
RNPAAEKMRL HGELDVNFNP QLASRETSDS SEPEEAPHTT DRRARRWRRA RLGSEEPSKE
PSSPSAQLRD LDTHQVSDDL SETDISNEAR DPQTLTDTTE EKRRNRLYEL AMKMSEKETS
SGEDQESEPK TESENQKESL SSEDNSQSVQ EELKKKFSAV SLCNISTEVL KVINATEELI
AGSTGPWESP QVPPDRQKGM FPRGTDQVRL DEQLTSLEEN VYLAAGTVYG LETQLTELED
AARCIHSGTD ETHLADLEDQ VATAAAQVHH AELQISDIES RISALTIAGL NIAPCVRFTR
RRDQKQRTQV QTIDTSRQQR RKLPAPPVKA EKIETSSVTT IKTFNHNFIL QGSSTNRTKE
RKGTTKDLME PALESAVMY
