ID   ALS2_PANTR              Reviewed;        1657 AA.
AC   Q5BIW4; Q29R55;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Alsin;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 protein homolog;
GN   Name=ALS2;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2]
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).
CC   -!- FUNCTION: May act as a GTPase regulator. Controls survival and growth
CC       of spinal motoneurons (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with ALS2CL
CC       (By similarity). {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BK005194; DAA05675.1; -; mRNA.
DR   RefSeq; NP_001073389.1; NM_001079920.1.
DR   AlphaFoldDB; Q5BIW4; -.
DR   STRING; 9598.ENSPTRP00000021899; -.
DR   PaxDb; Q5BIW4; -.
DR   GeneID; 470613; -.
DR   KEGG; ptr:470613; -.
DR   CTD; 57679; -.
DR   eggNOG; KOG0231; Eukaryota.
DR   eggNOG; KOG1426; Eukaryota.
DR   InParanoid; Q5BIW4; -.
DR   OrthoDB; 37470at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
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:0001662; P:behavioral fear response; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0007528; P:neuromuscular junction development; ISS:UniProtKB.
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:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR   GO; GO:0051036; P:regulation of endosome size; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0016050; P:vesicle organization; ISS:UniProtKB.
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; 5.
DR   PROSITE; PS51205; VPS9; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1657
FT                   /note="Alsin"
FT                   /id="PRO_0000080905"
FT   REPEAT          60..109
FT                   /note="RCC1 1"
FT   REPEAT          110..168
FT                   /note="RCC1 2"
FT   REPEAT          169..219
FT                   /note="RCC1 3"
FT   REPEAT          526..577
FT                   /note="RCC1 4"
FT   REPEAT          578..628
FT                   /note="RCC1 5"
FT   DOMAIN          690..885
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          901..1007
FT                   /note="PH"
FT   REPEAT          1049..1071
FT                   /note="MORN 1"
FT   REPEAT          1072..1094
FT                   /note="MORN 2"
FT   REPEAT          1100..1122
FT                   /note="MORN 3"
FT   REPEAT          1123..1145
FT                   /note="MORN 4"
FT   REPEAT          1151..1173
FT                   /note="MORN 5"
FT   REPEAT          1175..1197
FT                   /note="MORN 6"
FT   REPEAT          1198..1220
FT                   /note="MORN 7"
FT   REPEAT          1221..1244
FT                   /note="MORN 8"
FT   DOMAIN          1513..1657
FT                   /note="VPS9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT   REGION          432..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT   MOD_RES         510
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C5Y8"
FT   MOD_RES         533
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT   MOD_RES         1335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C5Y8"
SQ   SEQUENCE   1657 AA;  183737 MW;  2D585F9C57ADF8DD CRC64;
     MDSKKRSSTE AEGSKERGLV HIWQAGSFPI TPERLPGWGG KTVLQAALGV KHGVLLTEDG
     EVYSFGTLPW RSGPVEICPS SPILENALVG QYVVTVATGS FHSGAVTDNG VAYMWGENSA
     GQCAVANQQY VPEPNPVSIA DSEASPLLAV RILQLACGEE HTLALSISRE IWAWGTGCQL
     GLITTAFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PSQDLKPVPE RCNQCSQLLI
     TMTDKEDHVI ISDSHCCPLG VTLTESQAEN HASTALSPST ETLDRQEEVF ENTLVANDQS
     VATELNAVSA QITSSDAMSS QQNVMGTTEI SSARNIPSYP DTQAVNEYLR KLSDHSVRED
     SEHGEKPMPS QPLLEEAIPN LHSPPTTSTS ALNSLVVSCA SAVGVRVAAT YEAGALSLKK
     VMNFYSTTPC ETGAQAGSSA IGPEGLKDSR EEQVKQESMQ GKKSSSLVDI REEETEGGSR
     RLSLPGLLSQ VSPRLLRKAA RVKTRTVVLT PTYSGEADAL LPSLRTEVWT WGKGKEGQLG
     HGDVLPRLQP LCVKCLDGKE VIHLEAGGYH SLALTAKSQV YSWGSNTFGQ LGHSDFPTTV
     PRLAKISSEN GVWSVAAGRD YSLFLVDTED FQPGLYYSGR QDPTEGDNLP ENHSGSKTPV
     LLSCSKLGYI SRVTAGKDSY LALVDKNIMG YIASLHELAT TERRFYSKLS DIKSQILRPL
     LSLENLGTTT TVQLLQEVAS RFSKLCYLIG QHGASLSSFL HGVKEARSLV ILKHSSLFLD
     SYTEYCTSIT NFLVMGGFQL LAKPAIDFLN KNQELLQDLS EVNDENTQLM EILNTLFFLP
     IRRLHNYAKV LLKLATCFEV ASPEYQKLQD SSSCYECLAL HLGRKRKEAE YTLGFWKTFP
     GKMTDSLRKP ERRLLCESSN RALSLQHAGR FSVNWFILFN DALVHAQFST HHVFPLATLW
     AEPLSEEAGG VNGLKITTPE EQFTLISSTP QEKTKWLRAI SQAVDQALRG MSDLPPYGSG
     SSVQRQEPPI SRSAKYTFYK DPRLKDATYD GRWLSGKPHG RGVLKWPDGK MYSGMFRNGL
     EDGYGEYRIP NKAMNKEDHY VGHWKEGKMC GQGVYSYASG EVFEGCFQDN MRHGHGLLRS
     GKLTSSSPSM FIGQWVMDKK AGYGVFDDIT RGEKYMGMWQ DDVCQGNGVV VTQFGLYYEG
     NFHLNKMMGN GVLLSEDDTI YEGEFSDDWT LSGKGTLTMP NGDYIEGYFS GEWGSGIKIT
     GTYFKPSLYE SDKDRPKVFR KLRNLAVPAD EKWKAVFDEC WRQLGCEGPG QGEVWKAWDN
     IAVALTTSRR QHRDSPEILS RSQTQTLESL EFIPQHVGAF SVEKYDDIRK YLIKACDTPL
     HPLGRLVETL VAVYRMTYVG VGANRRLLQE AVKEIKSYLK RIFQLVRFLF PELPEEGSTI
     PLSAPLPTER KSFCTGKSDS RSESPEPGYV VTSSGLLLPV LLPRLYPPLF MLYALDNDRE
     EDIYWECVLR LNKQPDIALL GFLGVQRKFW PATLSILGES KKVLPTTKDA CFASAVECLQ
     QISTTFTPSD KLKVIQQTFE EISQSVLASL HEDFLWSMDD LFPVFLYVVL RARIRNLGSE
     VHLIEDLMDP YLQHGEQGIM FTTLKACYYQ IQREKLN