GenomeNet

Database: UniProt
Entry: A0A096MNG6_PAPAN
LinkDB: A0A096MNG6_PAPAN
Original site: A0A096MNG6_PAPAN 
ID   A0A096MNG6_PAPAN        Unreviewed;      1078 AA.
AC   A0A096MNG6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Cytospin-A {ECO:0000256|RuleBase:RU367063};
GN   Name=SPECC1L {ECO:0000313|Ensembl:ENSPANP00000001192.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000001192.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000001192.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000001192.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in cytokinesis and spindle organization. May play a
CC       role in actin cytoskeleton organization and microtubule stabilization
CC       and hence required for proper cell adhesion and migration.
CC       {ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC       {ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|RuleBase:RU367063}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|RuleBase:RU367063}. Cell junction, gap junction
CC       {ECO:0000256|RuleBase:RU367063}.
CC   -!- SIMILARITY: Belongs to the cytospin-A family.
CC       {ECO:0000256|RuleBase:RU367063}.
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   AlphaFoldDB; A0A096MNG6; -.
DR   Ensembl; ENSPANT00000021733.3; ENSPANP00000001192.2; ENSPANG00000007713.3.
DR   eggNOG; KOG4678; Eukaryota.
DR   GeneTree; ENSGT00940000153592; -.
DR   HOGENOM; CLU_009328_1_0_1; -.
DR   Proteomes; UP000028761; Chromosome 16.
DR   Bgee; ENSPANG00000007713; Expressed in thyroid gland and 67 other cell types or tissues.
DR   ExpressionAtlas; A0A096MNG6; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR036872; CH_dom_sf.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   PANTHER; PTHR23167:SF18; CYTOSPIN-A; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|RuleBase:RU367063};
KW   Cell division {ECO:0000256|RuleBase:RU367063};
KW   Cell junction {ECO:0000256|RuleBase:RU367063};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367063};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU367063};
KW   Gap junction {ECO:0000256|RuleBase:RU367063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761}.
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          243..270
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          400..441
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          488..805
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1078 AA;  120099 MW;  CF53B741650E9C74 CRC64;
     MKKASRSVGS VPKVSGISKT QTAEKVKPEN SSSASTGGKL VKPGTAASLS KTKSSDDLLA
     GMAGGVTVTN GVKGKKSTCP SAAPSASAPA MTTVESKSKI STGTASSTKR STSTGNKESS
     STRERLRERT RLNQSKKLPS AGQGANDVAL AKRSRSRTAT ECDVRMSKSK SDNQISDRAA
     LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGINEDHS EGDEKSEKET IMAHQPTDVE
     STLLQLQEQN TAIREELNQL KNENRMLKDR LNALGFSLEQ RLDNSEKLFG YQSLSPEITP
     GNQSDGGGTL TSSVEGSAPG SVEDLLSQDE NTLMDHQHSN SMDNLDSECS EVYQPLTSSD
     DALDAPSSSE SEGIPSIERS RKGSSGNASE VSVACLTERI HQMEENQHST SEELQATLQE
     LADLQQITQE LNSENERLGE EKVILMESLC QQSDKLEHFS RQIEYFRSLL DEHHISYVID
     EDVKSGRYME LEQRYMDLAE NARFEREQLL GVQQHLSNTL KMAEQDNKEA QEMIGALKER
     SHHMERIIES EQKGKAALAA TLEEYKATVA SDQIEMNRLK AQLENEKQKV AELYSIHNSG
     DKSDIQDLLE SVRLDKEKAE TLASSLQEDL AHTRNDANRL QDAIAKVEDE YRAFQEEAKK
     QIEDLNMTLE KLRSDLDEKE TERSDMKETI FELEDEVEQH RAVKLHDNLI ISDLENTVKK
     LQDQKHDMER EIKTLHRRLR EESAEWRQFQ ADLQTAVVIA NDIKSEAQEE IGDLKRRLHE
     AQEKNEKLTK ELEEIKSRKQ EEERGRVYNY MNAVERDLAA LRQGMGLSRR SSTSSEPTPT
     VKTLIKSFDS ASQVPNPAAA AIPRTPLSPS PMKTPPAAAV SPMQRHSISG PISTSKPLTA
     LSDKRPNYGE IPVQEHLLRT SSTSRPASLP RVPAMESAKT LSVSRRSSEE MKRDISAQEG
     ASPASLMAMG TTSPQLSLSS SPTASVTPTT RSRIREERKD PLSALAREYG GSKRNALLKW
     CQKKTEGYQR RNFMLAFQAA ESVGIKSTLD INEMVRTERP DWQNVMLYVT AIYKYFET
//
DBGET integrated database retrieval system