ALS2_RAT
ID ALS2_RAT Reviewed; 1651 AA.
AC P0C5Y8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alsin;
DE AltName: Full=Amyotrophic lateral sclerosis 2 protein homolog;
GN Name=Als2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION.
RX PubMed=16802292; DOI=10.1002/ana.20886;
RA Jacquier A., Buhler E., Schaefer M.K., Bohl D., Blanchard S., Beclin C.,
RA Haase G.;
RT "Alsin/Rac1 signaling controls survival and growth of spinal motoneurons.";
RL Ann. Neurol. 60:105-117(2006).
RN [3]
RP IDENTIFICATION.
RX PubMed=15686953; DOI=10.1016/j.nbd.2004.10.002;
RA Devon R.S., Schwab C., Topp J.D., Orban P.C., Yang Y.Z., Pape T.D.,
RA Helm J.R., Davidson T.L., Rogers D.A., Gros-Louis F., Rouleau G.,
RA Horazdovsky B.F., Leavitt B.R., Hayden M.R.;
RT "Cross-species characterization of the ALS2 gene and analysis of its
RT pattern of expression in development and adulthood.";
RL Neurobiol. Dis. 18:243-257(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-486; THR-504 AND
RP SER-1329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May act as a GTPase regulator (By similarity). Controls
CC survival and growth of spinal motoneurons. {ECO:0000250,
CC ECO:0000269|PubMed:16802292}.
CC -!- SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with ALS2CL
CC (By similarity). {ECO:0000250}.
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DR EMBL; AABR03068212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK005190; DAA05671.1; -; mRNA.
DR RefSeq; NP_001013431.1; NM_001013413.1.
DR RefSeq; XP_006245063.1; XM_006245001.3.
DR AlphaFoldDB; P0C5Y8; -.
DR SMR; P0C5Y8; -.
DR STRING; 10116.ENSRNOP00000036116; -.
DR iPTMnet; P0C5Y8; -.
DR PhosphoSitePlus; P0C5Y8; -.
DR PaxDb; P0C5Y8; -.
DR PRIDE; P0C5Y8; -.
DR GeneID; 363235; -.
DR KEGG; rno:363235; -.
DR UCSC; RGD:1310372; rat.
DR CTD; 57679; -.
DR RGD; 1310372; Als2.
DR VEuPathDB; HostDB:ENSRNOG00000023280; -.
DR eggNOG; KOG0231; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_003333_0_0_1; -.
DR InParanoid; P0C5Y8; -.
DR OMA; WFSGKPH; -.
DR OrthoDB; 37470at2759; -.
DR PhylomeDB; P0C5Y8; -.
DR TreeFam; TF331793; -.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:P0C5Y8; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000023280; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P0C5Y8; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0008219; P:cell death; IMP:RGD.
DR GO; GO:0016197; P:endosomal transport; ISO:RGD.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007041; P:lysosomal transport; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:RGD.
DR GO; GO:0001881; P:receptor recycling; ISO:RGD.
DR GO; GO:0051036; P:regulation of endosome size; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0016050; P:vesicle organization; ISO:RGD.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.130.10.30; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR Pfam; PF02493; MORN; 8.
DR Pfam; PF00415; RCC1; 4.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF02204; VPS9; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00698; MORN; 8.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50985; SSF50985; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 4.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1651
FT /note="Alsin"
FT /id="PRO_0000306085"
FT REPEAT 59..108
FT /note="RCC1 1"
FT REPEAT 109..167
FT /note="RCC1 2"
FT REPEAT 169..218
FT /note="RCC1 3"
FT REPEAT 519..570
FT /note="RCC1 4"
FT REPEAT 572..621
FT /note="RCC1 5"
FT DOMAIN 684..879
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 895..1001
FT /note="PH"
FT REPEAT 1043..1065
FT /note="MORN 1"
FT REPEAT 1066..1088
FT /note="MORN 2"
FT REPEAT 1094..1116
FT /note="MORN 3"
FT REPEAT 1117..1139
FT /note="MORN 4"
FT REPEAT 1145..1167
FT /note="MORN 5"
FT REPEAT 1169..1191
FT /note="MORN 6"
FT REPEAT 1192..1214
FT /note="MORN 7"
FT REPEAT 1215..1238
FT /note="MORN 8"
FT DOMAIN 1507..1651
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 444..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1651 AA; 182448 MW; 039F9225DFAFA1FC CRC64;
MDSKKKSSAE AEGSKERGLV HVWQAGSFSL TPERLPGWGG KTVLQAALGV KHGVLLTEDG
EVYSFGTLPW KSEAAEICPS SPLLESALVG HHVVTVATGS FHSGAVTESG VVYMWGENAA
GQCAVANQQY VSEPSPVSIS DSETSPLLAV RILQLACGEE HTLALSISRE IWAWGTGCQL
GLITTTFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PPQDLKPVPE RCNQCSQLLI
TMTDKEDHVI ISDSHCCPLG VTLSESQAEK HASTVTSPHP ETLDGQGEVF ENTVAEAELN
MGSDQTTSGS AISAQQNIVG MAEVSSARTA PSYPDTQTVT AYLQKLSEHS VKENHEREEK
LPQVQPLVEE AVPDLHSPPT TSTSALNSLV VSCASAVGVR VAATYEAGAL SLKKVMNFYS
TAPCEPGAPS GTASTGPESL KDLREEQVKQ ESLQGKKSSS LMDIREEESE GGSRRLSLPG
LLSQVSPRLL RKAARVKTRT VVLTPTYSGE ADALLPSLRT EVWTWGKGKE GQLGHGDVLP
RLQPLCVKCL DGKEVIHLEA GGSHSLALTA KSQVYSWGSN TFGQLGHSEF PTTVPRLSKV
SSESGVWSVA AGHGYSLFLV DTEDFQPGLY YSGRQDRAEG DTLPENPSGT TTPVLLSCSK
LGYISRVTAG KDSYLALVDK NIMGYIASLH ELATTERRFY SKLSEIKSQI LRPLLSLEHL
GTVTTVQLLQ EVASRFSKLC YLIGQHGASL SSYLQGMKEA RNLVIMKHSS LFLDSYTEYC
TSVSNFLVMG GSQLLAKPAI DFLNKNQELL QDLSEVNDEN TQLMEILNAL FFLPIRRLHN
YAKVLLKLAT CFEVTSPEYQ KLQDSSSCYE SLALHLGKKR KEAEYTLSFW KTFPGKMTDS
LRKPERRLLC ESSNRALSLQ HAGRFSVNWF ILFNDALVHA QFSTHHVFPL ATLWAEPLSE
ETGGVNGLKI TTPEEQFTLI SSTPQEKTKW LRAISQAVDQ ALRGTSDFPL YGGSSTVQRQ
EPPISRSAKY TFYKDTRLKD ATYDGRWLSG KPHGRGVLKW PDGKVYSGTF RNGLEDGYGE
YRIPNKALNK EDHYVGHWKE GKMCGQGVYS YASGEVFEGC FQDNMRHGHG LLRSGKLTSS
SPSMFIGQWV MDKKAGYGVF DDITRGEKYM GMWQDDACQG NGVVVTQFGL YYEGNFHLNK
MMGNGVLLSE DDTIYEGEFS DDWTLCGKGT LTMPNGDYIE GYFSGEWGSG IKITGTYFKP
SLYESDKDRP KAFRKLGNLA VAADEKWRAV FDECWRQLGC ESPGQGEVWK AWDNIAVALT
TNRRQHKDSP EILSRSQTQT LESLEYIPQH VGAFSVEKYD DIKKYLIKAC DTPLHPLGRL
VETLVAVYRM TYVGVGANRR LLQEAVKEIK SYLKRIFQLV RFLFPELPEE GSTVPLSAPL
PTGRRSFCTG KSDSRSESPE PGYVVTSSGL LLPVLLPRLY PPLFMLYALD NDREEDIYWE
CVLRLNKQPD IALLGFLGVQ RKFWPATLSI LGESKKVLPS TKDACFASAV ECLQQISTTF
TPSDKLKVIQ QTFEEISQSV LASLQEDFLW SMDDLFPVFL YVVLRARIRN LGSEVHLIED
LMDPYLQHGE QGIMFTTLKA CYYQIQREKL N
