ANR27_MOUSE
ID ANR27_MOUSE Reviewed; 1048 AA.
AC Q3UMR0; Q6KAU0; Q6P1F9; Q7TNY8; Q8BUD2; Q91W65;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ankyrin repeat domain-containing protein 27;
DE AltName: Full=VPS9 domain-containing protein;
DE AltName: Full=VPS9-ankyrin-repeat protein;
GN Name=Ankrd27; Synonyms=Varp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=16525121; DOI=10.1242/jcs.02810;
RA Zhang X., He X., Fu X.-Y., Chang Z.;
RT "Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome
RT dynamics.";
RL J. Cell Sci. 119:1053-1062(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1048 (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, INTERACTION WITH VAMP7, AND SUBCELLULAR LOCATION.
RX PubMed=19745841; DOI=10.1038/embor.2009.186;
RA Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C.,
RA Lanzetti L., Proux-Gillardeaux V., Galli T.;
RT "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in
RT neurite growth.";
RL EMBO Rep. 10:1117-1124(2009).
RN [7]
RP FUNCTION, INTERACTION WITH RAB32 AND RAB38, AND SUBCELLULAR LOCATION.
RX PubMed=19403694; DOI=10.1091/mbc.e08-12-1161;
RA Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.;
RT "Varp is a novel Rab32/38-binding protein that regulates Tyrp1 trafficking
RT in melanocytes.";
RL Mol. Biol. Cell 20:2900-2908(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, INTERACTION WITH RAB32; RAB38 AND VAMP7, AND MUTAGENESIS OF
RP GLN-509; TYR-550; TRP-575 AND TYR-577.
RX PubMed=21187289; DOI=10.1074/jbc.m110.191205;
RA Tamura K., Ohbayashi N., Ishibashi K., Fukuda M.;
RT "Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in the
RT trafficking of tyrosinase-related protein 1 in melanocytes.";
RL J. Biol. Chem. 286:7507-7521(2011).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-310; TYR-350; GLN-509 AND TYR-550.
RX PubMed=22171327; DOI=10.1091/mbc.e11-04-0324;
RA Ohbayashi N., Yatsu A., Tamura K., Fukuda M.;
RT "The Rab21-GEF activity of Varp, but not its Rab32/38 effector function, is
RT required for dendrite formation in melanocytes.";
RL Mol. Biol. Cell 23:669-678(2012).
RN [11]
RP FUNCTION.
RX PubMed=26620560; DOI=10.1074/jbc.m115.684043;
RA Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
RT "RUTBC1 functions as a GTPase-activating protein for Rab32/38 and regulates
RT melanogenic enzyme trafficking in melanocytes.";
RL J. Biol. Chem. 291:1427-1440(2016).
CC -!- FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and
CC Rab38 and regulate endosome dynamics (By similarity). May regulate the
CC participation of VAMP7 in membrane fusion events; in vitro inhibits
CC VAMP7-mediated SNARE complex formation by trapping VAMP7 in a closed,
CC fusogenically inactive conformation (By similarity). Involved in
CC peripheral melanosomal distribution of TYRP1 in melanocytes; the
CC function, which probably is implicating vesicle-trafficking, includes
CC cooperation with Rab32, Rab38 and VAMP7 (PubMed:19403694,
CC PubMed:21187289). Involved in the regulation of neurite growth; the
CC function seems to require its GEF activity, probably towards Rab21, and
CC VAMP7 but not Rab32/38 (PubMed:19745841, PubMed:22171327). Proposed to
CC be involved in Golgi sorting of VAMP7 and transport of VAMP7 vesicles
CC to the cell surface; the function seems to implicate kinesin heavy
CC chain isoform 5 proteins, GOLGA4, RAB21 and MACF1. Required for the
CC colocalization of VAMP7 and Rab21, probably on TGN sites (By
CC similarity). Involved in GLUT1 endosome-to-plasma membrane trafficking;
CC the function is dependent of association with VPS29 (By similarity).
CC Regulates the proper trafficking of melanogenic enzymes TYR, TYRP1 and
CC DCT/TYRP2 to melanosomes in melanocytes (PubMed:26620560).
CC {ECO:0000250|UniProtKB:Q96NW4, ECO:0000269|PubMed:19403694,
CC ECO:0000269|PubMed:21187289, ECO:0000269|PubMed:26620560}.
CC -!- SUBUNIT: Interacts with RAB21 (GDP-bound form), VPS29, KIF5A, KIF5C,
CC GOLGA4 (By similarity). Interacts with RAB32 (GTP-bound form), RAB38
CC (GTP-bound form), VAMP7 (PubMed:19403694, PubMed:21187289). Interacts
CC with low affinity with RAB5 (By similarity). ANKRD27:RAB32 heterodimers
CC can homodimerize to form tetramers (By similarity). Can interact with
CC RAB38 or RAB32, VPS29 and VAMP7 simultaneously (By similarity). A
CC decreased interaction with RAB32 seen in the presence of SGSM2 (By
CC similarity). {ECO:0000250|UniProtKB:Q96NW4,
CC ECO:0000269|PubMed:16525121, ECO:0000269|PubMed:19403694,
CC ECO:0000269|PubMed:21187289}.
CC -!- INTERACTION:
CC Q3UMR0; Q8QZZ8: Rab38; NbExp=5; IntAct=EBI-1993429, EBI-1993463;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q96NW4}.
CC Late endosome {ECO:0000250|UniProtKB:Q96NW4}. Cytoplasmic vesicle
CC membrane {ECO:0000250|UniProtKB:Q96NW4}. Lysosome
CC {ECO:0000250|UniProtKB:Q96NW4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96NW4}. Melanosome
CC {ECO:0000269|PubMed:19403694}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:19403694}. Note=Colocalizes with VAMP7 in transport
CC vesicles in the shaft of hippocampal neurons.
CC {ECO:0000269|PubMed:19745841}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UMR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMR0-2; Sequence=VSP_022792;
CC Name=3;
CC IsoId=Q3UMR0-3; Sequence=VSP_022791;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP94281.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY336500; AAP94281.1; ALT_FRAME; mRNA.
DR EMBL; AK085796; BAC39537.1; -; mRNA.
DR EMBL; AK144733; BAE26038.1; -; mRNA.
DR EMBL; BC016493; AAH16493.1; -; mRNA.
DR EMBL; BC065093; AAH65093.1; -; mRNA.
DR EMBL; AK131117; BAD21367.1; -; Transcribed_RNA.
DR CCDS; CCDS21154.1; -. [Q3UMR0-1]
DR RefSeq; NP_663608.3; NM_145633.3. [Q3UMR0-1]
DR RefSeq; NP_839994.1; NM_178263.3.
DR AlphaFoldDB; Q3UMR0; -.
DR SMR; Q3UMR0; -.
DR BioGRID; 232848; 3.
DR IntAct; Q3UMR0; 3.
DR MINT; Q3UMR0; -.
DR STRING; 10090.ENSMUSP00000041751; -.
DR iPTMnet; Q3UMR0; -.
DR PhosphoSitePlus; Q3UMR0; -.
DR EPD; Q3UMR0; -.
DR MaxQB; Q3UMR0; -.
DR PaxDb; Q3UMR0; -.
DR PRIDE; Q3UMR0; -.
DR ProteomicsDB; 281999; -. [Q3UMR0-1]
DR ProteomicsDB; 282000; -. [Q3UMR0-2]
DR ProteomicsDB; 282001; -. [Q3UMR0-3]
DR Antibodypedia; 47942; 86 antibodies from 23 providers.
DR DNASU; 245886; -.
DR Ensembl; ENSMUST00000040844; ENSMUSP00000041751; ENSMUSG00000034867. [Q3UMR0-1]
DR Ensembl; ENSMUST00000190503; ENSMUSP00000140259; ENSMUSG00000034867. [Q3UMR0-2]
DR GeneID; 245886; -.
DR KEGG; mmu:245886; -.
DR UCSC; uc009gkd.1; mouse. [Q3UMR0-1]
DR UCSC; uc012fin.1; mouse. [Q3UMR0-2]
DR CTD; 84079; -.
DR MGI; MGI:2444103; Ankrd27.
DR VEuPathDB; HostDB:ENSMUSG00000034867; -.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000157021; -.
DR HOGENOM; CLU_010760_0_1_1; -.
DR InParanoid; Q3UMR0; -.
DR OMA; LCHPLCT; -.
DR OrthoDB; 871322at2759; -.
DR PhylomeDB; Q3UMR0; -.
DR TreeFam; TF351261; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 245886; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ankrd27; mouse.
DR PRO; PR:Q3UMR0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UMR0; protein.
DR Bgee; ENSMUSG00000034867; Expressed in retinal neural layer and 222 other tissues.
DR ExpressionAtlas; Q3UMR0; baseline and differential.
DR Genevisible; Q3UMR0; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR GO; GO:0097422; C:tubular endosome; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 2.
DR Pfam; PF02204; VPS9; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Cytoplasmic vesicle;
KW Endosome; GTPase activation; Guanine-nucleotide releasing factor; Lysosome;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1048
FT /note="Ankyrin repeat domain-containing protein 27"
FT /id="PRO_0000274557"
FT DOMAIN 233..371
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REPEAT 396..426
FT /note="ANK 1"
FT REPEAT 462..491
FT /note="ANK 2"
FT REPEAT 495..524
FT /note="ANK 3"
FT REPEAT 528..557
FT /note="ANK 4"
FT REPEAT 564..593
FT /note="ANK 5"
FT REPEAT 597..627
FT /note="ANK 6"
FT REPEAT 668..698
FT /note="ANK 7"
FT REPEAT 742..771
FT /note="ANK 8"
FT REPEAT 775..804
FT /note="ANK 9"
FT REPEAT 808..837
FT /note="ANK 10"
FT REPEAT 841..870
FT /note="ANK 11"
FT REGION 1..372
FT /note="Sufficient for GEF activity towards RAB21"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT REGION 396..460
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT REGION 451..729
FT /note="Interaction with RAB32"
FT /evidence="ECO:0000269|PubMed:19403694"
FT REGION 451..600
FT /note="Interaction with RAB38"
FT /evidence="ECO:0000269|PubMed:19403694"
FT REGION 618..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..707
FT /note="Required for interaction with VAMP7"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4,
FT ECO:0000269|PubMed:19745841"
FT REGION 692..745
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT REGION 949..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT MOD_RES 1022
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT VAR_SEQ 630..670
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15449545"
FT /id="VSP_022791"
FT VAR_SEQ 670..724
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022792"
FT MUTAGEN 310
FT /note="D->A: Inhibits dendrite formation."
FT /evidence="ECO:0000269|PubMed:22171327"
FT MUTAGEN 350
FT /note="Y->A: Inhibits dendrite formation."
FT /evidence="ECO:0000269|PubMed:22171327"
FT MUTAGEN 509
FT /note="Q->A: Disrupts interaction with RAB32 and RAB38;
FT inhibits peripheral distribution of TYRP1 in melanocytes;
FT no effect on dendrite formation in melanocytes."
FT /evidence="ECO:0000269|PubMed:21187289,
FT ECO:0000269|PubMed:22171327"
FT MUTAGEN 550
FT /note="Y->A: Disrupts interaction with RAB32 and RAB38;
FT inhibits peripheral distribution of TYRP1 in melanocytes;
FT no effect on dendrite formation in melanocytes."
FT /evidence="ECO:0000269|PubMed:21187289,
FT ECO:0000269|PubMed:22171327"
FT MUTAGEN 575
FT /note="W->A: Impairs interaction with RAB32 and RAB38."
FT /evidence="ECO:0000269|PubMed:21187289"
FT MUTAGEN 577
FT /note="Y->A: Impairs interaction with RAB32 and RAB38."
FT /evidence="ECO:0000269|PubMed:21187289"
FT CONFLICT 281..310
FT /note="QQKLLCLRKVVQLMTQSPSQRVNLETMCAD -> TAEAAVPEEGGPAHDTIS
FT QPESELGDHVCR (in Ref. 2; BAC39537)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="TP -> PQ (in Ref. 4; BAD21367)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..377
FT /note="DAEGF -> VRSPC (in Ref. 3; AAH16493)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="P -> Q (in Ref. 2; BAE26038)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="K -> KV (in Ref. 4; BAD21367)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="S -> P (in Ref. 1; AAP94281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1048 AA; 116809 MW; 63636820D0CC4D2C CRC64;
MALYDEDLLK NPFYLALQKW RPDLCSKVAQ IHGIVLVPCR GSLPGSVQAS CQFESYVLVP
TEGHFQTLDG KAVVIEGNRI KLGAGFACLL SVPILFEETF YNEKEESFSI LCIAHPLERR
ETSEEPSAPA DPFSLKTIED VREFLGRHSE KFDKNIASFH RTFRECERKS LRHHIDSVNA
LYTKCLQQLL RDSHLKVLAK QEAQMNLMKQ AVEMYVHHDI YDLIFKYVGT MEASEDAAFN
KITRSLQDLQ QKDIGVKPEF SFNIPRAKRE LGQLNKCTSP QQKLLCLRKV VQLMTQSPSQ
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSSAKDELGY CLTSVEAAIE
YIRQGSLSTK TPDAEGFGDR LFLKQRMNLL SQMTSTPIDC LFKHIASGNQ KEVERLLSQD
DQDKDAMQKM CHPLCSCEDC EKLISGRLND PSVVTPFSRD DRGQTPLHVA ALCGQASLID
FLVSKGAVVN ATDYHGSTPL HLACQKGFQS VTLLLLHYKA STEVQDNNGN TPLHLACTYG
QEDCVKALVY YDVQACRLDI GNEKGDTALH IAARWGYEGI IETLLQNGAP TAVQNRLKET
PLKCALNSKI LSIMEAHHLS SDRRPRPSEV PAQSPTRSVD SISQGSSTSS FSSISVSFRQ
EEVKKDYREV EKLLRAVADG DLEMVRYLLE WTEDDLDDVE DAISTVDLEF CHPLCQCPKC
APAQKLARIS ANGLSVNVTN QDGFSPLHMA ALHGRTDLVP LLLKHGAYSG ARNTSQAVPL
HLACQQGHFQ VAKCLLDSNA KPNKKDLSGN TPLICACSAG HHEVAALLLQ HGASINACNN
KGNTALHEAV MGRHTLVVEL LLFYGASVDI LNKRQYTAAD CAEQDSKIME LLQVVPGCVA
SLDSVEEADH EGYVTVEIRR KWNPKMYNLP EEPLRRQFCL INPGGRFQER TSRETMGRDR
SVPDLAGRSL QEPEKQRVTG KQSDLSDLSR YQTSEEGNKG LPERPVSRQA APGHRPMVRR
HTVNDAAILQ VPEVTVHLTT HEASVPQS
