HHATL_MOUSE
ID HHATL_MOUSE Reviewed; 503 AA.
AC Q9D1G3; Q3TZE3; Q8R1K3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein-cysteine N-palmitoyltransferase HHAT-like protein;
DE AltName: Full=Glycerol uptake/transporter homolog;
DE AltName: Full=Hedgehog acyltransferase-like protein;
GN Name=Hhatl; Synonyms=Gup1, Kiaa1173;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Inner ear;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=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 [3]
RP FUNCTION, INTERACTION WITH SHH, AND SUBCELLULAR LOCATION.
RX PubMed=18081866; DOI=10.1111/j.1742-4658.2007.06202.x;
RA Abe Y., Kita Y., Niikura T.;
RT "Mammalian Gup1, a homolog of Saccharomyces cerevisiae glycerol
RT uptake/transporter 1, acts as a negative regulator for N-terminal
RT palmitoylation of Sonic hedgehog.";
RL FEBS J. 275:318-331(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: Negatively regulates N-terminal palmitoylation of SHH by
CC HHAT/SKN. {ECO:0000269|PubMed:18081866}.
CC -!- SUBUNIT: Interacts with SHH. {ECO:0000269|PubMed:18081866}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18081866}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18081866}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family. HHAT
CC subfamily. {ECO:0000305}.
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DR EMBL; AK003605; BAB22885.1; -; mRNA.
DR EMBL; AK157924; BAE34266.1; -; mRNA.
DR EMBL; BC024464; AAH24464.1; -; mRNA.
DR CCDS; CCDS23638.1; -.
DR RefSeq; NP_083371.2; NM_029095.2.
DR RefSeq; XP_006512442.1; XM_006512379.2.
DR RefSeq; XP_006512443.1; XM_006512380.3.
DR RefSeq; XP_006512444.1; XM_006512381.2.
DR AlphaFoldDB; Q9D1G3; -.
DR SMR; Q9D1G3; -.
DR IntAct; Q9D1G3; 1.
DR STRING; 10090.ENSMUSP00000035110; -.
DR TCDB; 2.A.50.1.2; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR iPTMnet; Q9D1G3; -.
DR PhosphoSitePlus; Q9D1G3; -.
DR MaxQB; Q9D1G3; -.
DR PaxDb; Q9D1G3; -.
DR PRIDE; Q9D1G3; -.
DR ProteomicsDB; 269567; -.
DR Antibodypedia; 2917; 80 antibodies from 21 providers.
DR DNASU; 74770; -.
DR Ensembl; ENSMUST00000035110; ENSMUSP00000035110; ENSMUSG00000032523.
DR Ensembl; ENSMUST00000163981; ENSMUSP00000131971; ENSMUSG00000032523.
DR GeneID; 74770; -.
DR KEGG; mmu:74770; -.
DR UCSC; uc009sdw.2; mouse.
DR CTD; 57467; -.
DR MGI; MGI:1922020; Hhatl.
DR VEuPathDB; HostDB:ENSMUSG00000032523; -.
DR eggNOG; KOG3860; Eukaryota.
DR GeneTree; ENSGT00530000063629; -.
DR HOGENOM; CLU_027533_0_0_1; -.
DR InParanoid; Q9D1G3; -.
DR OMA; MTVPQHR; -.
DR OrthoDB; 392243at2759; -.
DR PhylomeDB; Q9D1G3; -.
DR TreeFam; TF315826; -.
DR BioGRID-ORCS; 74770; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9D1G3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D1G3; protein.
DR Bgee; ENSMUSG00000032523; Expressed in vestibular membrane of cochlear duct and 99 other tissues.
DR ExpressionAtlas; Q9D1G3; baseline and differential.
DR Genevisible; Q9D1G3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0060262; P:negative regulation of N-terminal protein palmitoylation; IDA:UniProtKB.
DR InterPro; IPR032980; HHAT-like.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13285:SF19; PTHR13285:SF19; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..503
FT /note="Protein-cysteine N-palmitoyltransferase HHAT-like
FT protein"
FT /id="PRO_0000213131"
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 151
FT /note="S -> F (in Ref. 1; BAB22885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 56431 MW; 00D530244B7E288F CRC64;
MGIKTALPAA ELGLYSLVLS GALAYAGRGL LEASQDGAHR KAFRESVRPG WEYLGRKMDV
ADFEWVMWFT NFRNVIVFAL SGHVLFAKLC TMVAPQLRSW MYAVYGVLAV VGTMGPWYLL
LLLGHCMVLY VASLLGQRWL CLALGLASLA SFKVDPGISW QSGFVTGTFD LQDVLFHGGS
SFTVLRCTSF ALESCAHPDR RYSLADLLKY NFYLPFFFFG PIMTFDRFHA QVSQEPVRPE
GELWHIQAQA GLSAAAIVAV DVFFHFFYIL TIPSDLKFAS RLPDSALAGL AYSNLVYDWV
KAAVLFGVVN TVARLDHLDP PQPPKCITAL YVFGETHFDR GINDWLCKYV YDHIGGDHST
VIPELAASVA TFVVTTLWLG PCDIVYLWSV LNCFGLNFEL WVQKLAERGP LAQIEARLSE
QMSRRVRALC GAVNFWAIIM YNLVSLNSLE FTELVARRLI LTGFPQTTLA VLFVTYCGVQ
LVKERERSLA LEEEQRQDRE KLE
