HTR5B_MOUSE
ID HTR5B_MOUSE Reviewed; 2070 AA.
AC Q8C547; Q3TPS4; Q5DTY0; Q5PRF1; Q8C6W1; Q8C773;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=HEAT repeat-containing protein 5B;
GN Name=Heatr5b; Synonyms=Kiaa1414;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1283 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, Heart, Hippocampus, and Hypothalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 124-1452 (ISOFORM 1).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Component of clathrin-coated vesicles (By similarity).
CC Component of the aftiphilin/p200/gamma-synergin complex, which plays
CC roles in AP1G1/AP-1-mediated protein trafficking including the
CC trafficking of transferrin from early to recycling endosomes, and the
CC membrane trafficking of furin and the lysosomal enzyme cathepsin D
CC between the trans-Golgi network (TGN) and endosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2D3}.
CC -!- SUBUNIT: Self-associates (By similarity). Component of the
CC aftiphilin/p200/gamma-synergin complex, at least composed of
CC AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a
CC role in the AP1G1/AP-1-mediated protein trafficking from early to
CC recycling endosomes and between the trans-Golgi network (TGN) and
CC endosomes (By similarity). Within the complex interacts with
CC AFTPH/aftiphilin and SYNRG/gamma-synergin; the interactions are direct
CC (By similarity). Interacts with GGA1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2D3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9P2D3}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9P2D3}. Note=Localization at clathrin-
CC coated vesicles depends on AFTPH/aftiphilin.
CC {ECO:0000250|UniProtKB:Q9P2D3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C547-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C547-2; Sequence=VSP_029696;
CC Name=3;
CC IsoId=Q8C547-3; Sequence=VSP_029694, VSP_029695;
CC Name=4;
CC IsoId=Q8C547-4; Sequence=VSP_029693;
CC -!- SIMILARITY: Belongs to the HEATR5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35246.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90444.1; Type=Erroneous translation; Evidence={ECO:0000305};
CC Sequence=BAD90444.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE37661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK052391; BAC34972.1; -; mRNA.
DR EMBL; AK053037; BAC35246.1; ALT_FRAME; mRNA.
DR EMBL; AK079542; BAC37677.2; -; mRNA.
DR EMBL; AK164172; BAE37661.1; ALT_INIT; mRNA.
DR EMBL; AC151264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086652; AAH86652.1; -; mRNA.
DR EMBL; AK220390; BAD90444.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS37697.1; -. [Q8C547-1]
DR RefSeq; NP_001074648.1; NM_001081179.1. [Q8C547-1]
DR AlphaFoldDB; Q8C547; -.
DR IntAct; Q8C547; 2.
DR STRING; 10090.ENSMUSP00000094882; -.
DR iPTMnet; Q8C547; -.
DR PhosphoSitePlus; Q8C547; -.
DR SwissPalm; Q8C547; -.
DR EPD; Q8C547; -.
DR MaxQB; Q8C547; -.
DR PaxDb; Q8C547; -.
DR PeptideAtlas; Q8C547; -.
DR PRIDE; Q8C547; -.
DR ProteomicsDB; 273350; -. [Q8C547-1]
DR ProteomicsDB; 273351; -. [Q8C547-2]
DR ProteomicsDB; 273352; -. [Q8C547-3]
DR ProteomicsDB; 273353; -. [Q8C547-4]
DR Antibodypedia; 52336; 19 antibodies from 8 providers.
DR DNASU; 320473; -.
DR Ensembl; ENSMUST00000097281; ENSMUSP00000094882; ENSMUSG00000039414. [Q8C547-1]
DR GeneID; 320473; -.
DR KEGG; mmu:320473; -.
DR UCSC; uc008dpb.1; mouse. [Q8C547-4]
DR UCSC; uc008dpc.1; mouse. [Q8C547-1]
DR UCSC; uc008dpe.1; mouse. [Q8C547-3]
DR CTD; 54497; -.
DR MGI; MGI:2444098; Heatr5b.
DR VEuPathDB; HostDB:ENSMUSG00000039414; -.
DR eggNOG; KOG1822; Eukaryota.
DR GeneTree; ENSGT00390000006205; -.
DR HOGENOM; CLU_000652_0_0_1; -.
DR InParanoid; Q8C547; -.
DR OMA; ADTHNEE; -.
DR OrthoDB; 71064at2759; -.
DR PhylomeDB; Q8C547; -.
DR TreeFam; TF300706; -.
DR BioGRID-ORCS; 320473; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8C547; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8C547; protein.
DR Bgee; ENSMUSG00000039414; Expressed in primary oocyte and 221 other tissues.
DR ExpressionAtlas; Q8C547; baseline and differential.
DR Genevisible; Q8C547; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040108; Laa1/Sip1/HEATR5.
DR PANTHER; PTHR21663; PTHR21663; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..2070
FT /note="HEAT repeat-containing protein 5B"
FT /id="PRO_0000311995"
FT REPEAT 848..885
FT /note="HEAT 1"
FT REPEAT 1062..1099
FT /note="HEAT 2"
FT REPEAT 1290..1327
FT /note="HEAT 3"
FT MOD_RES 1737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2D3"
FT VAR_SEQ 1..1433
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_029693"
FT VAR_SEQ 802..804
FT /note="QML -> VKR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029694"
FT VAR_SEQ 805..2070
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029695"
FT VAR_SEQ 1059..2054
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029696"
FT CONFLICT 159
FT /note="S -> T (in Ref. 1; BAC35246)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="E -> V (in Ref. 1; BAE37661)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="D -> G (in Ref. 4; BAD90444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2070 AA; 224319 MW; 45297F223F744F73 CRC64;
MELAHSLLLN EEALAQITEA KRPVFIFEWL RFLDKVLVAA NKTDVKEKQK KLVEQLTGLI
SSSPGPPTRK LLAKNLAALY SIGDTYTVFQ TLDKCNDIIR SKDDTAAYLP TKLAAVACVG
AFYEKMGRML GSAFPETVNN LLKSLKSAES QGRSEILMSL QKVLTGLGGA AASSHRDIYK
NARSLLTDRS MAVRCAVAKC LLELQNEAVF MWTAELENVA TLCFKALENS NYGVRVAVSK
LLGTVMATAL MPKQATVMRQ NVKRATFDEV LELMATGFLR GGSGFLKSGG EMLKVGGSVN
REVRVGVTQA YVVFVTTLGG QWLERSFATF LSHVLDLVSH PRATQTHVDA VYSRRCVSFM
LRATVGSLLG EKAQIAAAKE ICQAIGKQMK AVEAVVNDTS SENKSGTADI AASQHVMVCA
LQELGSLVQS LNATASPLIQ EASIGLLEIV TSVLLHPSMA ARLAAAWCLR CVAVALPFQL
TPFLDRCAER LNNLKTSPEA VSGYSFAMAA LLGGVHQCPL GIPHAKGKMV VSIAEDLLRT
AAQNSRLSLQ RTQAGWLLLG ALMTLGPSVV RYHLPKMLLL WRNVFPRSLK ELEAEKARGD
SFTWQVTLEG RAGALCAMRS FVAHCPELLT EDAIRKLMTP IECAMTMMSH IPSVIKAHGA
HLKASAAMVR LRLYDILALL PPKTYEGSFN ALLRELVAEF TLTDNSANTT TSLLRSLCHY
DDSVLLGSWL QETDHKSIED QLQPNSASGS GALEHDPSSI YLRIPAGEAV PGPLPLGVSV
IDASVALFGV VFPHVSYKHR LQMLDHFAEC VKQAKGVRQQ AVQLNIFTAV LSALKGLAEN
KSTLGPEEVR KSALTLVMGA LDNPNPILRC AAGEALGRMA QVVGEASFIA RMAQYSFDKL
KSARDVVSRT GHSLALGCLH RYVGGIGSGQ HLKTSVSILL ALAQDGTSPE VQTWSLHSLA
LIVDSSGPMY RGYVEPTLSL VLTLLLTVPP SHTEVHQCLG RCLGAIITTV GPELQGNAAT
ISTIRSSCLV GCAITQDHSD SLVQAAAISC LQQLHMFAPR HVNLSSLVPS LCVHLCSSHL
LLRRAAVACL RQLAQREAAE VCEYAMSLAK NAGDKEISGG NVNPFTPGVS SRSDVHCRHQ
GVNITDTGLE GLLFGMLDRE TDRKLCSDIH DTLGHMLSSL AVEKLSHWLM LCKDVLAASS
DMSAATLLSS GKDEESEKKD EMDDDAMFTT LGEEDKSKPF VAPRWATRVF AADCLCRIIN
LCENSDQAHF DLALARSAKL RNPKNDLLVL HLSDLIRMAF MAATDHSNQL RMAGLQALED
IIKKFASVPE PEFPGHVILE QYQANVGAAL RPAFSQDTPS DIIAKACQVC STWIGSGVVS
DLNDLRRVHN LLVSSLDTVQ AGKGSSSQLY RESATTMEKL AVLKAWAEVY VVAMNIKKEA
ESKPKRAMNN PDDDDDDYGT IDELPPDSLI TLVQPELPTL SRLWLAALKD YALLTLPAEF
SSQLPPDGGA FYTPETIDTA RLHYRNSWAP ILHAVALWLN STGFISQEST EATTVSGVQK
RSPAVSLNQV PGAMASAKPL PEVNKDRMHL ILGVSIQFLC SPRPEEPIEH VTACLQALHT
LLGSPYARIH IAEDQLIGVE LLSVLHRLLL TWNPPSIQLL VTGVVQQIVR AAQDYLQEKR
NALNEEDMEK ESCPTLGEGG DTGGLIPGKS LVFATMELLM FILVRHMPHL STKMLDSPSH
TAMKTQLSEE SARLVAATVA ILSDLPSLCS PAGCMTILPT ILFLIARILK DTAIKSADNQ
VPPPVSAALQ GIKSIVTLSM AKTEDTQKQW TTLIRSTLAC ILEYSQPDDC MPAPDEVSTL
TAIALFLWSA SSEIIGVQSL QNGCMNRFKS ALNSCDPWVQ AKCYQLLLSV FQHSNRALST
PYIHSLAPLV VGKLKAVERH RPASSTELLA VQEGIKVLET LVALGEEQNR VQLLALLVPT
LISYLLDENS FASASSISKD LHEFALQNLM HIGPLYPHAF KTVMGAAPEL KARLETAVRA
SQASKAKAAA RQPAPTTHST PTIKLKTSFF
