OBSL1_RAT
ID OBSL1_RAT Reviewed; 1805 AA.
AC D3ZZ80;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Obscurin-like protein 1 {ECO:0000250|UniProtKB:O75147};
GN Name=Obsl1;
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] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21572988; DOI=10.1371/journal.pbio.1001060;
RA Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E.,
RA Gygi S.P., Harper J.W., Bonni A.;
RT "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi
RT morphology and dendrite patterning.";
RL PLoS Biol. 9:E1001060-E1001060(2011).
CC -!- FUNCTION: Core component of the 3M complex, a complex required to
CC regulate microtubule dynamics and genome integrity. It is unclear how
CC the 3M complex regulates microtubules, it could act by controlling the
CC level of a microtubule stabilizer (By similarity). Acts as a regulator
CC of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical
CC role in the ubiquitin ligase pathway that regulates Golgi morphogenesis
CC and dendrite patterning in brain. Required to localize CUL7 to the
CC Golgi apparatus in neurons. {ECO:0000250, ECO:0000269|PubMed:21572988}.
CC -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7,
CC CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the
CC interaction is direct. Interacts with FBXW8. Interacts (via N-terminal
CC Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the
CC interaction is direct (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75147}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75147}. Golgi
CC apparatus {ECO:0000250|UniProtKB:O75147}. Note=Colocalizes with CUL7 at
CC the Golgi apparatus in neurons. {ECO:0000250|UniProtKB:O75147}.
CC -!- TISSUE SPECIFICITY: Expressed in granule neurons, with levels
CC decreasing with neuronal maturation. {ECO:0000269|PubMed:21572988}.
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DR EMBL; AC112361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006226950.1; XM_006226888.2.
DR RefSeq; XP_006245367.1; XM_006245305.2.
DR AlphaFoldDB; D3ZZ80; -.
DR SMR; D3ZZ80; -.
DR STRING; 10116.ENSRNOP00000020673; -.
DR PaxDb; D3ZZ80; -.
DR PRIDE; D3ZZ80; -.
DR Ensembl; ENSRNOT00000020673; ENSRNOP00000020673; ENSRNOG00000015346.
DR GeneID; 363259; -.
DR CTD; 23363; -.
DR RGD; 1306073; Obsl1.
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000156702; -.
DR HOGENOM; CLU_000630_0_0_1; -.
DR InParanoid; D3ZZ80; -.
DR OMA; THRRCQA; -.
DR OrthoDB; 15947at2759; -.
DR PhylomeDB; D3ZZ80; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR PRO; PR:D3ZZ80; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000015346; Expressed in skeletal muscle tissue and 17 other tissues.
DR Genevisible; D3ZZ80; RN.
DR GO; GO:1990393; C:3M complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:RGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 19.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 13.
DR SMART; SM00409; IG; 17.
DR SMART; SM00408; IGc2; 14.
DR SUPFAM; SSF48726; SSF48726; 17.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 14.
PE 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Golgi apparatus; Immunoglobulin domain;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1805
FT /note="Obscurin-like protein 1"
FT /id="PRO_0000422123"
FT DOMAIN 12..100
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 128..225
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 240..330
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 339..425
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 517..615
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 720..800
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 804..891
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 902..982
FT /note="Ig-like 7"
FT /evidence="ECO:0000255"
FT DOMAIN 986..1075
FT /note="Ig-like 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1078..1165
FT /note="Ig-like 9"
FT /evidence="ECO:0000255"
FT DOMAIN 1176..1261
FT /note="Ig-like 10"
FT /evidence="ECO:0000255"
FT DOMAIN 1266..1351
FT /note="Ig-like 11"
FT /evidence="ECO:0000255"
FT DOMAIN 1355..1442
FT /note="Ig-like 12"
FT /evidence="ECO:0000255"
FT DOMAIN 1536..1628
FT /note="Ig-like 13"
FT /evidence="ECO:0000255"
FT DOMAIN 1702..1798
FT /note="Ig-like 14"
FT /evidence="ECO:0000255"
FT REGION 17..19
FT /note="Interaction with TTN"
FT /evidence="ECO:0000250|UniProtKB:O75147"
FT REGION 85..94
FT /note="Interaction with TTN"
FT /evidence="ECO:0000250|UniProtKB:O75147"
FT REGION 104..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75147"
FT DISULFID 33..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 267..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 362..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 738..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 829..879
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 920..970
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1011..1061
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1103..1153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1195..1245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1558..1608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1805 AA; 197865 MW; F5B9FBBD2DC719BC CRC64;
MKASSGDQGS PPCFLRFPRP VRVVSGAEAE LKCVVLGEPP PTVLWEKGGQ QLVASERLSF
PEDGAEHGLL LSGALPTDAG VYVCRARNAA GEAYAAAAVT VLEPPAPEPE PQSSECPPPP
PGTGEGAPVF LTGPQSQWVL RGAEVVLTCQ VGGLPEPKLY WEKDGMALDE VWDSSHYTLE
PDRGASDGGA SLTLRILAAR LPDSGVYVCH ARNAHGHAQA GALLQVHQPH ENPPQDPDEP
PVRVIEPLKC APKTFWVNEG KHAKFRCYVM GKPEPEIEWH LEGRPLLPDR RRLMYRDRDG
GFVLKVLYCQ AKDRGLYVCA ARNSAGQTLS AVQLHVKEPR LRFTRPLQDV EGREHGIVVL
ECKVPNSRIP TAWFREDQRL LPCRKYEQIE EGTVRRLVIH RLKADDDGVY LCEMRGRVRT
VANVTVKGPI LKRLPRKLDV LEGENAVLLV ETQEAGVQGC WSRDGEELPA TCQSSCGHMH
ALVLPGVTRE DAGEVTFSLG NSRTTTLLRV KCVKHSPPGP PVLVEMFKGQ KNTVLLTWKP
PEPPPETSFI YRLERQEVGS EDWIQCFSIE KAGAVEVPGD CVPTEGDYRF RICTVSEHGR
SPHVVFNGSA HLVPTARLVS GLEDVQVYDG EDAVFSLDLS TIIQGSWFLN GELLKNDEAE
GQVEPGALRY RIEQKGLQHR LILQTVKHQD NGALVGFICP GVQDSAALSI QESPVHILSP
QDKVLLTFTT SERVVLTCEL SRVDFPATWY KDGQKVEESE SLVVKMDGRK HRLILPEAQV
RDSGEFECRT EGISAFFSVT VQDPPVHIVD PQEHVFVHAI TSESVMLTCE VDREDAAVHW
YKDGQEVEES AVIVLEKEGP RHRLVLPAAQ PSDGGEFQCV VGDERAYFTV TITDVSSWIV
YPNGKVYVAA VRLERVVLTC ELCRPWAEVR WTKDGEEVLE SPALLLEKED TIRRLVLPSV
QLEDSGEYLC EIHDESASFT ITVTEPPVRI IYPQDEVTLH AVSLECVVLT CELSRVDAPV
RWYKDGLEVE ETEALVLQSD GPRRRLVLPA AQPEDGGEFV CDAGDDSAFF TVTVTAPPER
IVHPVARSLD LQFGAPGHVE LRCEVAPAGS QVRWYKDGLE VEVSDALQLG AEGPARTLTL
PHAQPEDAGE YVCETRDEAV TFNVSLAELP VQFLAPEAVP NPLCVVPGEP VMLSCELSRA
SAHVSWSHNG NPVKQGEGLE LRAEGPRRIL CIQAADLAHT GVYTCQSGTA PGAPSLSFNV
QVAEPPPVKL VSELTPLTVH EGDDATFQCE VSPPDAEVTW LRNGAIVTPG PQLEMVHSGS
SRTLIIRGCQ LKDAGTVTAR AGATDTSARL HVRETELLFL RRLQDVRAEE GQDVYLEVET
GRVGAPGAVR WLRGGEPLPL DSRLTTAQDG HVHRLSIHGV LLTDQGTYGC ESHHDRTLAR
LSVRPRQLRE LRPLEDVTVH EGGSATFQLE LSQEGVTGEW AQGGVRLHPG PKCHIHSEGR
THCLVLSGLG LADSGCISFT ADTLRCAARL TVREVPVTIV QGPQDLEVTE GDTATFECEL
SQTLADVIWE KDGQALSLSP RLRLQSLGTR RLLLLRRCSS SDAGTYCCAV GTARSGPARL
TVREREVSVL GELRSLSARE GDSATFECTV SESETTGRWE LGGRALRPGG RVRIRQEGKK
HILVLSELRT EDTGEVCFQA GPAQSLARLE VEALPLQMCR RPPREKTVLV DRRAVLEVTV
SRPGGHVCWM REGVELCPGS KYEMRSHGTT HSLVIHDVRP EDQGTYSCQA GQDSADTQLL
VEGDD
