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AR6P1_HUMAN
ID   AR6P1_HUMAN             Reviewed;         203 AA.
AC   Q15041; B7Z6S5; B7Z791; F5GXP4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=ADP-ribosylation factor-like protein 6-interacting protein 1;
DE            Short=ARL-6-interacting protein 1;
DE            Short=Aip-1;
DE   AltName: Full=Apoptotic regulator in the membrane of the endoplasmic reticulum {ECO:0000303|PubMed:12754298};
GN   Name=ARL6IP1;
GN   Synonyms=ARL6IP, ARMER {ECO:0000303|PubMed:12754298}, KIAA0069;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA   Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA   Kawarabayasi Y., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. II. The
RT   coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 1:223-229(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Esophagus, and Small intestine;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10995579; DOI=10.1006/geno.2000.6278;
RA   Pettersson M., Bessonova M., Gu H.F., Groop L.C., Jonsson J.I.;
RT   "Characterization, chromosomal localization, and expression during
RT   hematopoietic differentiation of the gene encoding Arl6ip, ADP-
RT   ribosylation-like factor-6 interacting protein (ARL6).";
RL   Genomics 68:351-354(2000).
RN   [6]
RP   FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12754298;
RA   Lui H.M., Chen J., Wang L., Naumovski L.;
RT   "ARMER, apoptotic regulator in the membrane of the endoplasmic reticulum, a
RT   novel inhibitor of apoptosis.";
RL   Mol. Cancer Res. 1:508-518(2003).
RN   [7]
RP   ERRATUM OF PUBMED:12754298.
RA   Lui H.M., Chen J., Wang L., Naumovski L.;
RL   Mol. Cancer Res. 1:630-630(2003).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=24076029; DOI=10.1016/j.febslet.2013.09.017;
RA   Kuroda M., Funasaki S., Saitoh T., Sasazawa Y., Nishiyama S., Umezawa K.,
RA   Simizu S.;
RT   "Determination of topological structure of ARL6ip1 in cells: identification
RT   of the essential binding region of ARL6ip1 for conophylline.";
RL   FEBS Lett. 587:3656-3660(2013).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATL1, SUBUNIT, AND
RP   TRANSMEMBRANE DOMAIN.
RX   PubMed=24262037; DOI=10.1042/bj20131186;
RA   Yamamoto Y., Yoshida A., Miyazaki N., Iwasaki K., Sakisaka T.;
RT   "Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-
RT   like fashion.";
RL   Biochem. J. 458:69-79(2014).
RN   [10]
RP   INTERACTION WITH TMEM33.
RX   PubMed=25612671;
RA   Urade T., Yamamoto Y., Zhang X., Ku Y., Sakisaka T.;
RT   "Identification and characterization of TMEM33 as a reticulon-binding
RT   protein.";
RL   Kobe J. Med. Sci. 60:E57-E65(2014).
RN   [11]
RP   INVOLVEMENT IN SPG61.
RX   PubMed=24482476; DOI=10.1126/science.1247363;
RA   Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA   Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA   Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA   Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA   Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA   Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA   Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA   Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA   Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA   Gleeson J.G.;
RT   "Exome sequencing links corticospinal motor neuron disease to common
RT   neurodegenerative disorders.";
RL   Science 343:506-511(2014).
RN   [12]
RP   VARIANT SPG61 38-ARG--GLU-203 DEL.
RX   PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA   Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA   AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA   El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA   Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA   Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA   Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA   Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA   Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA   Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT   "Autozygome and high throughput confirmation of disease genes candidacy.";
RL   Genet. Med. 21:736-742(2019).
CC   -!- FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate
CC       transport by increasing its affinity for glutamate in a PKC activity-
CC       dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1
CC       probably by reducing its interaction with ARL6IP5, a negative regulator
CC       of SLC1A1/EAAC1-mediated glutamate transport (By similarity). Plays a
CC       role in the formation and stabilization of endoplasmic reticulum
CC       tubules (PubMed:24262037). Negatively regulates apoptosis, possibly by
CC       modulating the activity of caspase-9 (CASP9). Inhibits cleavage of
CC       CASP9-dependent substrates and downstream markers of apoptosis but not
CC       CASP9 itself (PubMed:12754298). May be involved in protein transport,
CC       membrane trafficking, or cell signaling during hematopoietic maturation
CC       (PubMed:10995579). {ECO:0000250|UniProtKB:Q9JKW0,
CC       ECO:0000269|PubMed:12754298, ECO:0000269|PubMed:24262037,
CC       ECO:0000303|PubMed:10995579}.
CC   -!- SUBUNIT: Homooligomer (PubMed:24262037). Heterodimer with ARL6IP5.
CC       Interacts with ARL6 (By similarity). Interacts with TMEM33
CC       (PubMed:25612671). Interacts with ATL1 (PubMed:24262037).
CC       {ECO:0000250|UniProtKB:Q9JKW0, ECO:0000269|PubMed:24262037,
CC       ECO:0000269|PubMed:25612671}.
CC   -!- INTERACTION:
CC       Q15041; Q96CM8: ACSF2; NbExp=8; IntAct=EBI-714543, EBI-2876502;
CC       Q15041; Q13520: AQP6; NbExp=3; IntAct=EBI-714543, EBI-13059134;
CC       Q15041; Q15041: ARL6IP1; NbExp=4; IntAct=EBI-714543, EBI-714543;
CC       Q15041; Q8NEA5: C19orf18; NbExp=3; IntAct=EBI-714543, EBI-18323646;
CC       Q15041; Q9Y5P4: CERT1; NbExp=5; IntAct=EBI-714543, EBI-739994;
CC       Q15041; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-714543, EBI-11156432;
CC       Q15041; Q9NR28: DIABLO; NbExp=9; IntAct=EBI-714543, EBI-517508;
CC       Q15041; Q9NZN3: EHD3; NbExp=3; IntAct=EBI-714543, EBI-2870749;
CC       Q15041; P54849: EMP1; NbExp=3; IntAct=EBI-714543, EBI-4319440;
CC       Q15041; P51116: FXR2; NbExp=3; IntAct=EBI-714543, EBI-740459;
CC       Q15041; Q05329: GAD2; NbExp=6; IntAct=EBI-714543, EBI-9304251;
CC       Q15041; O95995: GAS8; NbExp=3; IntAct=EBI-714543, EBI-1052570;
CC       Q15041; Q9H4A6: GOLPH3; NbExp=3; IntAct=EBI-714543, EBI-2465479;
CC       Q15041; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-714543, EBI-739467;
CC       Q15041; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-714543, EBI-11955647;
CC       Q15041; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-714543, EBI-13345167;
CC       Q15041; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-714543, EBI-18053395;
CC       Q15041; Q9BT40: INPP5K; NbExp=5; IntAct=EBI-714543, EBI-749162;
CC       Q15041; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-714543, EBI-2816356;
CC       Q15041; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-714543, EBI-373355;
CC       Q15041; Q6N075: MFSD5; NbExp=3; IntAct=EBI-714543, EBI-3920969;
CC       Q15041; O14880: MGST3; NbExp=3; IntAct=EBI-714543, EBI-724754;
CC       Q15041; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-714543, EBI-11988931;
CC       Q15041; Q96E29: MTERF3; NbExp=3; IntAct=EBI-714543, EBI-7825321;
CC       Q15041; Q9HB07: MYG1; NbExp=6; IntAct=EBI-714543, EBI-709754;
CC       Q15041; Q9H115: NAPB; NbExp=3; IntAct=EBI-714543, EBI-3921185;
CC       Q15041; Q9ULP0: NDRG4; NbExp=3; IntAct=EBI-714543, EBI-10323810;
CC       Q15041; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-714543, EBI-11978907;
CC       Q15041; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-714543, EBI-741158;
CC       Q15041; Q9Y3D7: PAM16; NbExp=3; IntAct=EBI-714543, EBI-721147;
CC       Q15041; Q5JS98: PBX3; NbExp=3; IntAct=EBI-714543, EBI-10244393;
CC       Q15041; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-714543, EBI-79165;
CC       Q15041; P43378: PTPN9; NbExp=3; IntAct=EBI-714543, EBI-742898;
CC       Q15041; Q14088: RAB33A; NbExp=3; IntAct=EBI-714543, EBI-744685;
CC       Q15041; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-714543, EBI-14065960;
CC       Q15041; Q86VR2: RETREG3; NbExp=7; IntAct=EBI-714543, EBI-10192441;
CC       Q15041; Q99942: RNF5; NbExp=3; IntAct=EBI-714543, EBI-348482;
CC       Q15041; Q9NQC3: RTN4; NbExp=3; IntAct=EBI-714543, EBI-715945;
CC       Q15041; O00560: SDCBP; NbExp=3; IntAct=EBI-714543, EBI-727004;
CC       Q15041; Q9HC62: SENP2; NbExp=3; IntAct=EBI-714543, EBI-714881;
CC       Q15041; Q8N114-3: SHISA5; NbExp=3; IntAct=EBI-714543, EBI-13369834;
CC       Q15041; P34897: SHMT2; NbExp=6; IntAct=EBI-714543, EBI-352908;
CC       Q15041; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-714543, EBI-18159983;
CC       Q15041; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-714543, EBI-17295964;
CC       Q15041; Q13596: SNX1; NbExp=4; IntAct=EBI-714543, EBI-2822329;
CC       Q15041; Q8N5Z3: SNX10; NbExp=3; IntAct=EBI-714543, EBI-10266928;
CC       Q15041; Q9Y5X0: SNX10; NbExp=6; IntAct=EBI-714543, EBI-10329478;
CC       Q15041; Q9Y5W9: SNX11; NbExp=6; IntAct=EBI-714543, EBI-10329449;
CC       Q15041; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-714543, EBI-1752602;
CC       Q15041; Q9UMY4-1: SNX12; NbExp=3; IntAct=EBI-714543, EBI-22419305;
CC       Q15041; Q9NRS6: SNX15; NbExp=4; IntAct=EBI-714543, EBI-725924;
CC       Q15041; O60749: SNX2; NbExp=3; IntAct=EBI-714543, EBI-1046690;
CC       Q15041; O60493: SNX3; NbExp=3; IntAct=EBI-714543, EBI-727209;
CC       Q15041; O95219: SNX4; NbExp=3; IntAct=EBI-714543, EBI-724909;
CC       Q15041; Q9Y5X2: SNX8; NbExp=3; IntAct=EBI-714543, EBI-1752557;
CC       Q15041; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-714543, EBI-742688;
CC       Q15041; Q96DR4: STARD4; NbExp=3; IntAct=EBI-714543, EBI-17217258;
CC       Q15041; E5KS60: SUCLA2; NbExp=3; IntAct=EBI-714543, EBI-10176959;
CC       Q15041; Q9P2R7: SUCLA2; NbExp=6; IntAct=EBI-714543, EBI-2269898;
CC       Q15041; Q9BW92: TARS2; NbExp=3; IntAct=EBI-714543, EBI-1045099;
CC       Q15041; Q00059: TFAM; NbExp=3; IntAct=EBI-714543, EBI-1049924;
CC       Q15041; Q6PL24: TMED8; NbExp=3; IntAct=EBI-714543, EBI-11603430;
CC       Q15041; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-714543, EBI-8638294;
CC       Q15041; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-714543, EBI-10314986;
CC       Q15041; P61165: TMEM258; NbExp=3; IntAct=EBI-714543, EBI-12019210;
CC       Q15041; A0A384ME17: TUFM; NbExp=6; IntAct=EBI-714543, EBI-12261790;
CC       Q15041; P49411: TUFM; NbExp=3; IntAct=EBI-714543, EBI-359097;
CC       Q15041; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-714543, EBI-10180829;
CC       Q15041; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-714543, EBI-1055364;
CC       Q15041; Q96P53: WDFY2; NbExp=3; IntAct=EBI-714543, EBI-9478589;
CC       Q15041; Q9Y4P8: WIPI2; NbExp=3; IntAct=EBI-714543, EBI-719396;
CC       Q15041; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-714543, EBI-751253;
CC       Q15041; Q9BQ24: ZFYVE21; NbExp=6; IntAct=EBI-714543, EBI-2849569;
CC       Q15041; P0DTC6: 6; Xeno; NbExp=3; IntAct=EBI-714543, EBI-25475897;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000269|PubMed:10995579}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10995579}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12754298, ECO:0000269|PubMed:24076029,
CC       ECO:0000269|PubMed:24262037}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:24076029}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9JKW0}. Note=Predominantly localized to
CC       intracytoplasmic membranes. Preferentially localizes at the ER tubules
CC       and the edge of the ER sheets, both of which are characterized by a
CC       high membrane curvature. {ECO:0000269|PubMed:24262037}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q15041-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15041-2; Sequence=VSP_057297;
CC       Name=3;
CC         IsoId=Q15041-3; Sequence=VSP_057298;
CC   -!- TISSUE SPECIFICITY: Expressed in all hematopoietic cell lineages, but
CC       the highest level of expression is found in early myeloid progenitor
CC       cells. Expressed in brain, bone marrow, thymus and lung. Expressed at
CC       low level in liver, kidney and spleen. Not detected in heart.
CC       {ECO:0000269|PubMed:10995579}.
CC   -!- DEVELOPMENTAL STAGE: Down-regulated during myeloid differentiation.
CC   -!- INDUCTION: Down-regulated by apoptotic stimuli.
CC       {ECO:0000269|PubMed:12754298}.
CC   -!- DOMAIN: The transmembrane domains are required for its ability to shape
CC       the endoplasmic reticulum membrane into tubules.
CC       {ECO:0000269|PubMed:24262037}.
CC   -!- DISEASE: Spastic paraplegia 61, autosomal recessive (SPG61)
CC       [MIM:615685]: A complicated form of spastic paraplegia with polysensory
CC       and motor neuropathy. Spastic paraplegia is a neurodegenerative
CC       disorder characterized by a slow, gradual, progressive weakness and
CC       spasticity of the lower limbs. Rate of progression and the severity of
CC       symptoms are quite variable. Initial symptoms may include difficulty
CC       with balance, weakness and stiffness in the legs, muscle spasms, and
CC       dragging the toes when walking. In some forms of the disorder, bladder
CC       symptoms (such as incontinence) may appear, or the weakness and
CC       stiffness may spread to other parts of the body.
CC       {ECO:0000269|PubMed:24482476, ECO:0000269|PubMed:30237576}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the ARL6ip family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA06683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D31885; BAA06683.1; ALT_INIT; mRNA.
DR   EMBL; AK300869; BAH13361.1; -; mRNA.
DR   EMBL; AK301636; BAH13527.1; -; mRNA.
DR   EMBL; AC138811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010281; AAH10281.1; -; mRNA.
DR   CCDS; CCDS10572.1; -. [Q15041-1]
DR   CCDS; CCDS81951.1; -. [Q15041-2]
DR   RefSeq; NP_001300787.1; NM_001313858.1. [Q15041-2]
DR   RefSeq; NP_055976.1; NM_015161.2. [Q15041-1]
DR   AlphaFoldDB; Q15041; -.
DR   BioGRID; 116812; 108.
DR   IntAct; Q15041; 84.
DR   MINT; Q15041; -.
DR   STRING; 9606.ENSP00000306788; -.
DR   iPTMnet; Q15041; -.
DR   PhosphoSitePlus; Q15041; -.
DR   SwissPalm; Q15041; -.
DR   BioMuta; ARL6IP1; -.
DR   DMDM; 14424435; -.
DR   EPD; Q15041; -.
DR   jPOST; Q15041; -.
DR   MassIVE; Q15041; -.
DR   MaxQB; Q15041; -.
DR   PaxDb; Q15041; -.
DR   PeptideAtlas; Q15041; -.
DR   PRIDE; Q15041; -.
DR   ProteomicsDB; 24482; -.
DR   ProteomicsDB; 60389; -. [Q15041-1]
DR   Antibodypedia; 11964; 286 antibodies from 31 providers.
DR   DNASU; 23204; -.
DR   Ensembl; ENST00000304414.12; ENSP00000306788.7; ENSG00000170540.15. [Q15041-1]
DR   Ensembl; ENST00000546206.6; ENSP00000440048.2; ENSG00000170540.15. [Q15041-2]
DR   GeneID; 23204; -.
DR   KEGG; hsa:23204; -.
DR   MANE-Select; ENST00000304414.12; ENSP00000306788.7; NM_015161.3; NP_055976.1.
DR   UCSC; uc002dfl.2; human. [Q15041-1]
DR   CTD; 23204; -.
DR   DisGeNET; 23204; -.
DR   GeneCards; ARL6IP1; -.
DR   HGNC; HGNC:697; ARL6IP1.
DR   HPA; ENSG00000170540; Low tissue specificity.
DR   MalaCards; ARL6IP1; -.
DR   MIM; 607669; gene.
DR   MIM; 615685; phenotype.
DR   neXtProt; NX_Q15041; -.
DR   OpenTargets; ENSG00000170540; -.
DR   Orphanet; 401780; Autosomal recessive spastic paraplegia type 61.
DR   PharmGKB; PA162376894; -.
DR   VEuPathDB; HostDB:ENSG00000170540; -.
DR   eggNOG; ENOG502QTTI; Eukaryota.
DR   GeneTree; ENSGT00940000154937; -.
DR   HOGENOM; CLU_100749_0_0_1; -.
DR   InParanoid; Q15041; -.
DR   OMA; VWYEYLF; -.
DR   PhylomeDB; Q15041; -.
DR   TreeFam; TF105477; -.
DR   PathwayCommons; Q15041; -.
DR   SignaLink; Q15041; -.
DR   BioGRID-ORCS; 23204; 17 hits in 1079 CRISPR screens.
DR   ChiTaRS; ARL6IP1; human.
DR   GeneWiki; ARL6IP1; -.
DR   GenomeRNAi; 23204; -.
DR   Pharos; Q15041; Tbio.
DR   PRO; PR:Q15041; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q15041; protein.
DR   Bgee; ENSG00000170540; Expressed in pigmented layer of retina and 205 other tissues.
DR   ExpressionAtlas; Q15041; baseline and differential.
DR   Genevisible; Q15041; HS.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006613; P:cotranslational protein targeting to membrane; IBA:GO_Central.
DR   GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IDA:UniProtKB.
DR   GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR   GO; GO:0002038; P:positive regulation of L-glutamate import across plasma membrane; ISS:UniProtKB.
DR   GO; GO:1903371; P:regulation of endoplasmic reticulum tubular network organization; IMP:CACAO.
DR   InterPro; IPR033301; ARL6IP.
DR   PANTHER; PTHR20952:SF3; PTHR20952:SF3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Disease variant; Endoplasmic reticulum;
KW   Hereditary spastic paraplegia; Membrane; Neurodegeneration;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..203
FT                   /note="ADP-ribosylation factor-like protein 6-interacting
FT                   protein 1"
FT                   /id="PRO_0000064655"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..65
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..203
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..29
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057297"
FT   VAR_SEQ         105..156
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057298"
FT   VARIANT         38..203
FT                   /note="Missing (in SPG61; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:30237576"
FT                   /id="VAR_082139"
FT   CONFLICT        110
FT                   /note="S -> I (in Ref. 2; BAH13527)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  23363 MW;  CE914D8FC9609FC6 CRC64;
     MAEGDNRSTN LLAAETASLE EQLQGWGEVM LMADKVLRWE RAWFPPAIMG VVSLVFLIIY
     YLDPSVLSGV SCFVMFLCLA DYLVPILAPR IFGSNKWTTE QQQRFHEICS NLVKTRRRAV
     GWWKRLFTLK EEKPKMYFMT MIVSLAAVAW VGQQVHNLLL TYLIVTSLLL LPGLNQHGII
     LKYIGMAKRE INKLLKQKEK KNE
 
 
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