RIMS1_HUMAN
ID RIMS1_HUMAN Reviewed; 1692 AA.
AC Q86UR5; A7MBN6; B7Z2M0; B7Z2Q9; B7Z3S3; B7Z6S2; E7EX08; E9PCB7; E9PCZ1;
AC E9PF48; E9PHF5; E9PHR1; O15048; Q5JY21; Q5JY25; Q5SZK1; Q8TDY9; Q8TDZ5;
AC Q9HBA1; Q9HBA2; Q9HBA3; Q9HBA4; Q9HBA5; Q9HBA6;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 1;
DE AltName: Full=Rab-3-interacting molecule 1;
DE Short=RIM 1;
DE AltName: Full=Rab-3-interacting protein 2;
GN Name=RIMS1; Synonyms=KIAA0340, RAB3IP2, RIM1; ORFNames=Nbla00761;
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), ALTERNATIVE SPLICING, AND VARIANT
RP CORD7 HIS-820.
RX PubMed=12659814; DOI=10.1016/s0888-7543(03)00010-7;
RA Johnson S., Halford S., Morris A.G., Patel R.J., Wilkie S.E.,
RA Hardcastle A.J., Moore A.T., Zhang K., Hunt D.M.;
RT "Genomic organisation and alternative splicing of human RIM1, a gene
RT implicated in autosomal dominant cone-rod dystrophy (CORD7).";
RL Genomics 81:304-314(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Neuroblastoma;
RA Aoyama M., Asai K., Shishikura T., Ohira M., Inuzuka H., Morohashi A.,
RA Kato T., Nakagawara A.;
RT "Identification of the alternative form of human RIM.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9; 10; 11; 12 AND 13).
RC TISSUE=Brain, Small intestine, and Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [MRNA] OF 776-1692 (ISOFORMS 3; 4; 5; 6; 7 AND 8),
RP MUTAGENESIS OF 796-LYS-LYS-797 AND 1591-ARG-ARG-1592, AND INTERACTION WITH
RP SNAP25; SYT1 AND CACNA1B.
RC TISSUE=Brain;
RX PubMed=11438518; DOI=10.1074/jbc.m100929200;
RA Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G.,
RA Regazzi R.;
RT "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25,
RT and synaptotagmin.";
RL J. Biol. Chem. 276:32756-32762(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677; SER-1680; SER-1683 AND
RP SER-1692, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
RN [11]
RP STRUCTURE BY NMR OF 585-694.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of human KIAA0340 protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Rab effector involved in exocytosis (By similarity). May act
CC as scaffold protein that regulates neurotransmitter release at the
CC active zone. Essential for maintaining normal probability of
CC neurotransmitter release and for regulating release during short-term
CC synaptic plasticity (By similarity). Plays a role in dendrite formation
CC by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q99NE5,
CC ECO:0000269|PubMed:23999003}.
CC -!- SUBUNIT: Binds RAB3A, RAB3B and RAB3D that have been activated by GTP-
CC binding. Interacts with RAB3C, RAB10, RAB26 AND RAB37. Binds UNC13A.
CC Interacts with TSPOAP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4.
CC Interacts with ERC1 (By similarity). Binds SNAP25, SYT1 and CACNA1B.
CC Interaction with SYT1 is enhanced by calcium ions. Interaction with
CC SNAP25 is weaker in the presence of calcium ions. {ECO:0000250,
CC ECO:0000269|PubMed:11438518}.
CC -!- INTERACTION:
CC Q86UR5; P00519: ABL1; NbExp=2; IntAct=EBI-1043236, EBI-375543;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=RIM1 alpha;
CC IsoId=Q86UR5-1; Sequence=Displayed;
CC Name=2; Synonyms=RIM short form;
CC IsoId=Q86UR5-2; Sequence=VSP_008165;
CC Name=3; Synonyms=RIM long form, Rab3 interacting protein variant 2;
CC IsoId=Q86UR5-3; Sequence=VSP_008164, VSP_008167, VSP_008171;
CC Name=4; Synonyms=Rab3 interacting protein variant 1;
CC IsoId=Q86UR5-4; Sequence=VSP_008166, VSP_008167;
CC Name=5; Synonyms=Rab3 interacting protein variant 3;
CC IsoId=Q86UR5-5; Sequence=VSP_008161, VSP_008163, VSP_008170;
CC Name=6; Synonyms=Rab3 interacting protein variant 4;
CC IsoId=Q86UR5-6; Sequence=VSP_008164, VSP_008168, VSP_008169;
CC Name=7; Synonyms=Rab3 interacting protein variant 5;
CC IsoId=Q86UR5-7; Sequence=VSP_008161, VSP_008164, VSP_008167,
CC VSP_008169;
CC Name=8; Synonyms=Rab3 interacting protein variant 6;
CC IsoId=Q86UR5-8; Sequence=VSP_008161, VSP_008162, VSP_008169;
CC Name=9;
CC IsoId=Q86UR5-9; Sequence=VSP_043177, VSP_043178, VSP_008164,
CC VSP_043179, VSP_043180, VSP_008169;
CC Name=10;
CC IsoId=Q86UR5-10; Sequence=VSP_045486, VSP_008164, VSP_043179,
CC VSP_043180, VSP_008169;
CC Name=11;
CC IsoId=Q86UR5-11; Sequence=VSP_045485;
CC Name=12;
CC IsoId=Q86UR5-12; Sequence=VSP_046796, VSP_008161, VSP_008164,
CC VSP_043179, VSP_043180;
CC Name=13;
CC IsoId=Q86UR5-13; Sequence=VSP_046796, VSP_008164, VSP_008167,
CC VSP_008169;
CC -!- TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003).
CC Detected in brain and retina (PubMed:23999003).
CC {ECO:0000269|PubMed:23999003}.
CC -!- PTM: Phosphorylated by BRSK1. {ECO:0000250}.
CC -!- DISEASE: Cone-rod dystrophy 7 (CORD7) [MIM:603649]: An inherited
CC retinal dystrophy characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:12659814}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20798.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI39600.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI42135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY190519; AAO38848.1; -; mRNA.
DR EMBL; AB045726; BAB87121.1; -; mRNA.
DR EMBL; AB051866; BAB87242.1; -; mRNA.
DR EMBL; AB002338; BAA20798.1; ALT_INIT; mRNA.
DR EMBL; AK296303; BAH12309.1; -; mRNA.
DR EMBL; AK294868; BAH11906.1; -; mRNA.
DR EMBL; AK295001; BAH11945.1; -; mRNA.
DR EMBL; AK300853; BAH13358.1; -; mRNA.
DR EMBL; AK309185; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL160405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590011; CAI16961.1; -; Genomic_DNA.
DR EMBL; AL034373; CAI16961.1; JOINED; Genomic_DNA.
DR EMBL; AL390056; CAI16961.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI16961.1; JOINED; Genomic_DNA.
DR EMBL; AL034373; CAI20558.1; -; Genomic_DNA.
DR EMBL; AL390056; CAI20558.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI20558.1; JOINED; Genomic_DNA.
DR EMBL; AL590011; CAI20558.1; JOINED; Genomic_DNA.
DR EMBL; AL390056; CAI21554.1; -; Genomic_DNA.
DR EMBL; AL034373; CAI21554.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI21554.1; JOINED; Genomic_DNA.
DR EMBL; AL590011; CAI21554.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI39598.1; -; Genomic_DNA.
DR EMBL; AL034373; CAI39598.1; JOINED; Genomic_DNA.
DR EMBL; AL390056; CAI39598.1; JOINED; Genomic_DNA.
DR EMBL; AL590011; CAI39598.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI39600.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035633; CAI39600.1; JOINED; Genomic_DNA.
DR EMBL; AL445256; CAI39604.1; -; Genomic_DNA.
DR EMBL; AL035633; CAI39604.1; JOINED; Genomic_DNA.
DR EMBL; AL035633; CAI42135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL445256; CAI42135.1; JOINED; Genomic_DNA.
DR EMBL; AL035633; CAI42139.1; -; Genomic_DNA.
DR EMBL; AL445256; CAI42139.1; JOINED; Genomic_DNA.
DR EMBL; BC151853; AAI51854.1; -; mRNA.
DR EMBL; BC152435; AAI52436.1; -; mRNA.
DR EMBL; AF263305; AAG23162.1; -; mRNA.
DR EMBL; AF263306; AAG23163.1; -; mRNA.
DR EMBL; AF263307; AAG23164.1; -; mRNA.
DR EMBL; AF263308; AAG23165.1; -; mRNA.
DR EMBL; AF263309; AAG23166.1; -; mRNA.
DR EMBL; AF263310; AAG23167.1; -; mRNA.
DR CCDS; CCDS47449.1; -. [Q86UR5-1]
DR CCDS; CCDS55029.1; -. [Q86UR5-13]
DR CCDS; CCDS55030.1; -. [Q86UR5-12]
DR CCDS; CCDS55031.1; -. [Q86UR5-9]
DR CCDS; CCDS55032.1; -. [Q86UR5-10]
DR CCDS; CCDS55033.1; -. [Q86UR5-11]
DR RefSeq; NP_001161879.1; NM_001168407.1. [Q86UR5-12]
DR RefSeq; NP_001161880.1; NM_001168408.1. [Q86UR5-13]
DR RefSeq; NP_001161881.1; NM_001168409.1. [Q86UR5-10]
DR RefSeq; NP_001161882.1; NM_001168410.1. [Q86UR5-9]
DR RefSeq; NP_001161883.1; NM_001168411.1. [Q86UR5-11]
DR RefSeq; NP_055804.2; NM_014989.5. [Q86UR5-1]
DR RefSeq; XP_011533917.2; XM_011535615.2.
DR PDB; 2CSS; NMR; -; A=585-692.
DR PDBsum; 2CSS; -.
DR AlphaFoldDB; Q86UR5; -.
DR SMR; Q86UR5; -.
DR BioGRID; 116646; 20.
DR IntAct; Q86UR5; 7.
DR STRING; 9606.ENSP00000428417; -.
DR GlyGen; Q86UR5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86UR5; -.
DR PhosphoSitePlus; Q86UR5; -.
DR BioMuta; RIMS1; -.
DR DMDM; 34395763; -.
DR EPD; Q86UR5; -.
DR jPOST; Q86UR5; -.
DR MassIVE; Q86UR5; -.
DR MaxQB; Q86UR5; -.
DR PaxDb; Q86UR5; -.
DR PeptideAtlas; Q86UR5; -.
DR PRIDE; Q86UR5; -.
DR ProteomicsDB; 19415; -.
DR ProteomicsDB; 19549; -.
DR ProteomicsDB; 20026; -.
DR ProteomicsDB; 20521; -.
DR ProteomicsDB; 69870; -. [Q86UR5-1]
DR ProteomicsDB; 69871; -. [Q86UR5-2]
DR ProteomicsDB; 69872; -. [Q86UR5-3]
DR ProteomicsDB; 69873; -. [Q86UR5-4]
DR ProteomicsDB; 69874; -. [Q86UR5-5]
DR ProteomicsDB; 69875; -. [Q86UR5-6]
DR ProteomicsDB; 69876; -. [Q86UR5-7]
DR ProteomicsDB; 69877; -. [Q86UR5-8]
DR ProteomicsDB; 69878; -. [Q86UR5-9]
DR Antibodypedia; 49157; 22 antibodies from 11 providers.
DR DNASU; 22999; -.
DR Ensembl; ENST00000264839.11; ENSP00000264839.7; ENSG00000079841.19. [Q86UR5-4]
DR Ensembl; ENST00000401910.7; ENSP00000385649.3; ENSG00000079841.19. [Q86UR5-12]
DR Ensembl; ENST00000414192.2; ENSP00000402273.2; ENSG00000079841.19. [Q86UR5-11]
DR Ensembl; ENST00000425662.6; ENSP00000411235.2; ENSG00000079841.19. [Q86UR5-10]
DR Ensembl; ENST00000491071.6; ENSP00000430101.1; ENSG00000079841.19. [Q86UR5-3]
DR Ensembl; ENST00000517827.5; ENSP00000428367.1; ENSG00000079841.19. [Q86UR5-9]
DR Ensembl; ENST00000517960.5; ENSP00000429959.1; ENSG00000079841.19. [Q86UR5-5]
DR Ensembl; ENST00000518273.5; ENSP00000430408.1; ENSG00000079841.19. [Q86UR5-6]
DR Ensembl; ENST00000520567.5; ENSP00000430502.1; ENSG00000079841.19. [Q86UR5-7]
DR Ensembl; ENST00000521978.6; ENSP00000428417.1; ENSG00000079841.19. [Q86UR5-1]
DR Ensembl; ENST00000522291.5; ENSP00000430932.1; ENSG00000079841.19. [Q86UR5-8]
DR Ensembl; ENST00000523963.5; ENSP00000428328.1; ENSG00000079841.19. [Q86UR5-13]
DR GeneID; 22999; -.
DR KEGG; hsa:22999; -.
DR MANE-Select; ENST00000521978.6; ENSP00000428417.1; NM_014989.7; NP_055804.2.
DR UCSC; uc003pga.5; human. [Q86UR5-1]
DR CTD; 22999; -.
DR DisGeNET; 22999; -.
DR GeneCards; RIMS1; -.
DR HGNC; HGNC:17282; RIMS1.
DR HPA; ENSG00000079841; Tissue enriched (brain).
DR MalaCards; RIMS1; -.
DR MIM; 603649; phenotype.
DR MIM; 606629; gene.
DR neXtProt; NX_Q86UR5; -.
DR OpenTargets; ENSG00000079841; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA38220; -.
DR VEuPathDB; HostDB:ENSG00000079841; -.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00940000155134; -.
DR HOGENOM; CLU_001061_1_0_1; -.
DR InParanoid; Q86UR5; -.
DR OMA; NRGRWSP; -.
DR PhylomeDB; Q86UR5; -.
DR TreeFam; TF321703; -.
DR PathwayCommons; Q86UR5; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR SignaLink; Q86UR5; -.
DR SIGNOR; Q86UR5; -.
DR BioGRID-ORCS; 22999; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; RIMS1; human.
DR EvolutionaryTrace; Q86UR5; -.
DR GeneWiki; RIMS1; -.
DR GenomeRNAi; 22999; -.
DR Pharos; Q86UR5; Tbio.
DR PRO; PR:Q86UR5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86UR5; protein.
DR Bgee; ENSG00000079841; Expressed in cerebellar cortex and 138 other tissues.
DR ExpressionAtlas; Q86UR5; baseline and differential.
DR Genevisible; Q86UR5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048786; C:presynaptic active zone; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0030695; F:GTPase regulator activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IDA:UniProtKB.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; TAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0061025; P:membrane fusion; NAS:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ParkinsonsUK-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; NAS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:ParkinsonsUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0046903; P:secretion; NAS:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; PTHR12157; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cone-rod dystrophy; Differentiation; Disease variant; Exocytosis; Membrane;
KW Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Repeat; Sensory transduction; Synapse; Transport;
KW Vision; Zinc; Zinc-finger.
FT CHAIN 1..1692
FT /note="Regulating synaptic membrane exocytosis protein 1"
FT /id="PRO_0000190198"
FT DOMAIN 22..182
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 605..691
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 742..865
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1538..1656
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 110..170
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NE5"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..1473
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045485"
FT VAR_SEQ 1..607
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045486"
FT VAR_SEQ 1..559
FT /note="MSSAVGPRGPRPPTVPPPMQELPDLSHLTEEERNIIMAVMDRQKEEEEKEEA
FT MLKCVVRDMAKPAACKTPRNAENQPHQPSPRLHQQFESYKEQVRKIGEEARRYQGEHKD
FT DAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQE
FT ILTKSGAWFFGSGPQQTSQDGTLSDTATGAGSEVPREKKARLQERSRSQTPLSTAAASS
FT QDAAPPSAPPDRSKGAEPSQQALGPEQKQASSRSRSEPPRERKKTPGLSEQNGKGALKS
FT ERKRVPKTSAQPVEGAVEERERKERRESRRLEKGRSQDYPDTPEKRDEGKAADEEKQRK
FT EEDYQTRYRSDPNLARYPVKPPPEEQQMRMHARVSRARHERRHSDVALPRTEAGAALPE
FT GKAGKRAPAAARASPPDSPRAYSAERTAETRAPGAKQLTNHSPPAPRHGPVPAEAPELK
FT AQEPLRKQSRLDPSSAVLMRKAKREKVETMLRNDSLSSDQSESVRPSPPKPHRSKRGGK
FT KRQMSVSSSEEEGVSTPEYTSCEDVELESESVSEK -> MCAPGIHVSSEGWEEVRSVD
FT SEEGTIEARRAVA (in isoform 12 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046796"
FT VAR_SEQ 1..18
FT /note="MSSAVGPRGPRPPTVPPP -> MFAGFLQFLLLHTLHSGT (in isoform
FT 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043177"
FT VAR_SEQ 19..559
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043178"
FT VAR_SEQ 924
FT /note="Missing (in isoform 5, isoform 7, isoform 8 and
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:11438518,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008161"
FT VAR_SEQ 1018..1245
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11438518"
FT /id="VSP_008162"
FT VAR_SEQ 1038..1244
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11438518"
FT /id="VSP_008163"
FT VAR_SEQ 1039..1102
FT /note="Missing (in isoform 3, isoform 6, isoform 7, isoform
FT 9, isoform 10, isoform 12 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:11438518,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_008164"
FT VAR_SEQ 1040..1692
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9205841, ECO:0000303|Ref.2"
FT /id="VSP_008165"
FT VAR_SEQ 1065..1102
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11438518"
FT /id="VSP_008166"
FT VAR_SEQ 1133..1245
FT /note="Missing (in isoform 3, isoform 4, isoform 7 and
FT isoform 13)"
FT /evidence="ECO:0000303|PubMed:11438518,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_008167"
FT VAR_SEQ 1133..1160
FT /note="Missing (in isoform 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043179"
FT VAR_SEQ 1161..1245
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11438518"
FT /id="VSP_008168"
FT VAR_SEQ 1185..1245
FT /note="Missing (in isoform 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043180"
FT VAR_SEQ 1284..1455
FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform
FT 9, isoform 10 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:11438518,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008169"
FT VAR_SEQ 1377..1385
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11438518"
FT /id="VSP_008170"
FT VAR_SEQ 1540..1573
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11438518, ECO:0000303|Ref.2"
FT /id="VSP_008171"
FT VARIANT 820
FT /note="R -> H (in CORD7; dbSNP:rs121918302)"
FT /evidence="ECO:0000269|PubMed:12659814"
FT /id="VAR_016804"
FT MUTAGEN 796..797
FT /note="RR->AA: Abolishes interaction with SYT1 and
FT CACNA1B."
FT /evidence="ECO:0000269|PubMed:11438518"
FT MUTAGEN 1591..1592
FT /note="KK->AA: Abolishes interaction with SYT1 and
FT CACNA1B."
FT /evidence="ECO:0000269|PubMed:11438518"
FT CONFLICT 157
FT /note="V -> Y (in Ref. 5; CAI16961)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..494
FT /note="Missing (in Ref. 2; BAB87121/BAB87242, 3; BAA20798
FT and 6; AAI51854/AAI52436)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="P -> S (in Ref. 4; BAH11945)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="Q -> R (in Ref. 4; BAH11906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1609
FT /note="V -> A (in Ref. 4; BAH13358)"
FT /evidence="ECO:0000305"
FT CONFLICT 1662
FT /note="S -> P (in Ref. 4; AK309185)"
FT /evidence="ECO:0000305"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 591..602
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 616..625
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 629..638
FT /evidence="ECO:0007829|PDB:2CSS"
FT HELIX 643..646
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:2CSS"
FT HELIX 669..678
FT /evidence="ECO:0007829|PDB:2CSS"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:2CSS"
FT STRAND 685..691
FT /evidence="ECO:0007829|PDB:2CSS"
SQ SEQUENCE 1692 AA; 189073 MW; 0A96642DC832C15E CRC64;
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MAKPAACKTP RNAENQPHQP SPRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICH
KTKFADGCGH LCSYCRTKFC ARCGGRVSLR SNNEDKVVMW VCNLCRKQQE ILTKSGAWFF
GSGPQQTSQD GTLSDTATGA GSEVPREKKA RLQERSRSQT PLSTAAASSQ DAAPPSAPPD
RSKGAEPSQQ ALGPEQKQAS SRSRSEPPRE RKKTPGLSEQ NGKGALKSER KRVPKTSAQP
VEGAVEERER KERRESRRLE KGRSQDYPDT PEKRDEGKAA DEEKQRKEED YQTRYRSDPN
LARYPVKPPP EEQQMRMHAR VSRARHERRH SDVALPRTEA GAALPEGKAG KRAPAAARAS
PPDSPRAYSA ERTAETRAPG AKQLTNHSPP APRHGPVPAE APELKAQEPL RKQSRLDPSS
AVLMRKAKRE KVETMLRNDS LSSDQSESVR PSPPKPHRSK RGGKKRQMSV SSSEEEGVST
PEYTSCEDVE LESESVSEKG DLDYYWLDPA TWHSRETSPI SSHPVTWQPS KEGDRLIGRV
ILNKRTTMPK DSGALLGLKV VGGKMTDLGR LGAFITKVKK GSLADVVGHL RAGDEVLEWN
GKPLPGATNE EVYNIILESK SEPQVEIIVS RPIGDIPRIP ESSHPPLESS SSSFESQKME
RPSISVISPT SPGALKDAPQ VLPGQLSVKL WYDKVGHQLI VNVLQATDLP ARVDGRPRNP
YVKMYFLPDR SDKSKRRTKT VKKILEPKWN QTFVYSHVHR RDFRERMLEI TVWDQPRVQE
EESEFLGEIL IELETALLDD EPHWYKLQTH DESSLPLPQP SPFMPRRHIH GESSSKKLQR
SQRISDSDIS DYEVDDGIGV VPPVGYRSSA RESKSTTLTV PEQQRTTHHR SRSVSPHRGN
DQGKPRSRLP NVPLQRSLDE IHPTRRSRSP TRHHDASRSP VDHRTRDVDS QYLSEQDSEL
LMLPRAKRGR SAECLHTTRH LVRHYKTLPP KMPLLQSSSH WNIYSSILPA HTKTKSVTRQ
DISLHHECFN STVLRFTDEI LVSELQPFLD RARSASTNCL RPDTSLHSPE RERGRWSPSL
DRRRPPSPRI QIQHASPEND RHSRKSERSS IQKQTRKGTA SDAERVLPTC LSRRGHAAPR
ATDQPVIRGK HPARSRSSEH SSIRTLCSMH HLVPGGSAPP SPLLTRMHRQ RSPTQSPPAD
TSFSSRRGRQ LPQVPVRSGS IEQASLVVEE RTRQMKMKVH RFKQTTGSGS SQELDREQYS
KYNIHKDQYR SCDNVSAKSS DSDVSDVSAI SRTSSASRLS STSFMSEQSE RPRGRISSFT
PKMQGRRMGT SGRSIMKSTS VSGEMYTLEH NDGSQSDTAV GTVGAGGKKR RSSLSAKVVA
IVSRRSRSTS QLSQTESGHK KLKSTIQRST ETGMAAEMRK MVRQPSREST DGSINSYSSE
GNLIFPGVRL GADSQFSDFL DGLGPAQLVG RQTLATPAMG DIQIGMEDKK GQLEVEVIRA
RSLTQKPGSK STPAPYVKVY LLENGACIAK KKTRIARKTL DPLYQQSLVF DESPQGKVLQ
VIVWGDYGRM DHKCFMGVAQ ILLEELDLSS MVIGWYKLFP PSSLVDPTLT PLTRRASQSS
LESSTGPPCI RS
