SRCA_RABIT
ID SRCA_RABIT Reviewed; 472 AA.
AC P13666; G1TFF2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sarcalumenin {ECO:0000303|PubMed:2762314};
DE Flags: Precursor;
GN Name=SRL;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=2762314; DOI=10.1073/pnas.86.16.6047;
RA Leberer E., Charuk J.H.M., Green N.M., Maclennan D.H.;
RT "Molecular cloning and expression of cDNA encoding a lumenal calcium
RT binding glycoprotein from sarcoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6047-6051(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=2521635; DOI=10.1016/s0021-9258(18)94092-5;
RA Leberer E., Charuk J.H.M., Clarke D.M., Green N.M., Zubrycka-Gaarn E.,
RA McLennan D.H.;
RT "Molecular cloning and expression of cDNA encoding the 53,000-dalton
RT glycoprotein of rabbit skeletal muscle sarcoplasmic reticulum.";
RL J. Biol. Chem. 264:3484-3493(1989).
RN [3] {ECO:0000312|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000312|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:2521635, ECO:0000269|PubMed:2762314}. Sarcoplasmic
CC reticulum membrane {ECO:0000269|PubMed:2521635,
CC ECO:0000269|PubMed:2762314}; Peripheral membrane protein
CC {ECO:0000269|PubMed:2521635, ECO:0000269|PubMed:2762314}. Note=May
CC associate with the sarcoplasmic reticulum membrane, via a calcium-
CC dependent mechanism. {ECO:0000269|PubMed:2521635,
CC ECO:0000269|PubMed:2762314}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=53 kDa {ECO:0000303|PubMed:2521635};
CC IsoId=P13666-2; Sequence=Displayed;
CC Name=2; Synonyms=160 kDa {ECO:0000303|PubMed:2762314};
CC IsoId=P13666-1; Sequence=VSP_060765;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle.
CC {ECO:0000269|PubMed:2521635, ECO:0000269|PubMed:2762314}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2521635,
CC ECO:0000269|PubMed:2762314}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; M25750; AAA31189.1; -; mRNA.
DR EMBL; J04480; AAA60730.1; -; mRNA.
DR PIR; A33280; A33280.
DR PIR; A33312; A33312.
DR RefSeq; NP_001075750.1; NM_001082281.1.
DR RefSeq; XP_008247813.1; XM_008249591.2. [P13666-2]
DR AlphaFoldDB; P13666; -.
DR SMR; P13666; -.
DR STRING; 9986.ENSOCUP00000015642; -.
DR Ensembl; ENSOCUT00000028857; ENSOCUP00000015642; ENSOCUG00000025140. [P13666-1]
DR Ensembl; ENSOCUT00000055593; ENSOCUP00000031954; ENSOCUG00000025140. [P13666-2]
DR GeneID; 100009112; -.
DR KEGG; ocu:100009112; -.
DR CTD; 6345; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000157834; -.
DR HOGENOM; CLU_017595_4_0_1; -.
DR InParanoid; P13666; -.
DR OMA; MEVTEVH; -.
DR OrthoDB; 377342at2759; -.
DR TreeFam; TF324008; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000025140; Expressed in skeletal muscle tissue and 15 other tissues.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF16880; EHD_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..472
FT /note="Sarcalumenin"
FT /id="PRO_0000022413"
FT DOMAIN 89..330
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 99..106
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 127..128
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 189..192
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 254..257
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 277
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 20
FT /note="E -> ELQVPASGGTEDVGNLLENHFSAGDASLEEKERALYADAAPRDENLL
FT LHYPDGREAESAERTTAGAPPAAPGPGSEPEASLPNASATESAPPGDATGPREEQGPAA
FT ASALPPGGDEGSLQEERQELSSGEGPGEEAAGLGLPSEGAASGETQGQAGGGKVPKEAE
FT GVLGDSPVQGAAAETAEPEASGIAPSSEDEQIHTLEGEGKGSPGPDHGPTELDGTPDGA
FT SAGEEPKADLDTEARERAEDQHQVHTLETEGKGGPGPHQGPAEVDGGPDTVSVGESLEA
FT REGAEDQGKPSPGQEAGPAAAEAGTEPGGTKHSEEEGMEQDRPPEGQVPVMRQDEGGEA
FT SSEEEGDEEGGSEEEEGDPSEEDSGEDSGDGASSEEAGAASEEASGTAGLGEEETQPST
FT EGLDSGPAGSQAQDTEAEEPEEGHQGPESPITAPQE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060765"
FT CONFLICT 38
FT /note="E -> Q (in Ref. 1; AAA31189)"
FT /evidence="ECO:0000305"
FT CARBOHYD P13666-1:102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT P13666-1:170
FT /note="T -> S (in Ref. 1; AAA31189)"
FT /evidence="ECO:0000305"
FT CONFLICT P13666-1:315
FT /note="G -> M (in Ref. 1; AAA31189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 54451 MW; C0A49B9E00233557 CRC64;
MRALLLFCFV ASLLLSGQAE ETEDVSEEVP MRDRSHIEKT LMLNEDKPTD DFSAVLQRLR
KIYHSSIKPL EQSYKYNELR QHEITDGEIT SKPMVLFLGP WSVGKSTMIN YLLGLENTRY
QLYTGAEPTT SEFTVLMHGP KLKTIEGIVM AADSARSFSP LEKFGQNFLE KLIGIEVPHK
LLERVTFVDT PGIIENRKQQ ERGYPFNDVC QWFIDRADLI FVVFDPTKLD VGLELETLFR
QLKGRESQIR IILNKADNLA TQMLMRVYGA LFWSLAPLIN VTEPPRVYVS SFWPQEYKPD
THRELFLREE ISLLEDLNQV IENRLENKIA FIRQHAIRVR IHALLVDRYL QTYKDKMTFF
SDGELVFKDI VEDPDKFYIF KTILAKTNVS KFDLPNREAY KDFFGINPIS SFKLLSQQCS
YMGGCFLEKI ERAITQELPS LLGSLGLGKN PGALNCDKTG CGETPKNRYK KH
