CYTSA_TETNG
ID CYTSA_TETNG Reviewed; 1113 AA.
AC Q2KN95; Q4SA63;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cytospin-A;
DE AltName: Full=SPECC1-like protein;
DE AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1-like;
GN Name=specc1l; Synonyms=cytsa; ORFNames=GSTENG00021593001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Ye T., Chen Y.;
RT "Characterization of cytospin A as a multiple coiled coil protein involved
RT in cytokinesis and spindle organization.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cell junction, gap junction
CC {ECO:0000250}. Note=Colocalizes with beta-tubulin, acetylated alpha-
CC tubulin and F-actin. Also observed in a ring around gamma-tubulin
CC containing centrioles possibly in the microtubule organizing center (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG02469.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AY884300; AAX84191.1; -; mRNA.
DR EMBL; CAAE01014692; CAG02469.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2KN95; -.
DR SMR; Q2KN95; -.
DR STRING; 99883.ENSTNIP00000014389; -.
DR Ensembl; ENSTNIT00000014588; ENSTNIP00000014389; ENSTNIG00000011443.
DR KEGG; tng:GSTEN00021593G001; -.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q2KN95; -.
DR OMA; RTSMENN; -.
DR TreeFam; TF316716; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR040166; CYTSA.
DR PANTHER; PTHR23167:SF18; PTHR23167:SF18; 1.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Gap junction; Reference proteome.
FT CHAIN 1..1113
FT /note="Cytospin-A"
FT /id="PRO_0000231025"
FT DOMAIN 1007..1112
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 220..259
FT /evidence="ECO:0000255"
FT COILED 379..433
FT /evidence="ECO:0000255"
FT COILED 473..791
FT /evidence="ECO:0000255"
FT COMPBIAS 60..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 122034 MW; 8D04420496AFCF2E CRC64;
MKKSVRPAAS KVSGERGKPE VAGNAAAGKP ASKSSTAAPL SKVKSSDDLL AAMAGGNPAS
CNAVSKSKRT TSVGTTASTL DSKPKTASGT TSKRLASSLS KETNLTRDRL RTSRASANKK
QSAAGPVGGD AASGKRSRGQ TLAESEGRMS KSKSDGQISD KVALETKVKD LLGLAKSKDV
EILHLRSELR DMRAQLGLGG EEPQEGAVEE EKPHVSAITA ADVESTLILL QEQNQAIREE
LNLLKSENRM LKDRLNALGF SLEQRLDGSD KLFSYASLSP DLAAGSGQSD GGGTGTLASS
VEGSAPGSLE DLLTGHQHGG SADNLDSESS EVYQAVTSSD DALDAPSGAS SSSESECAPS
RERSRRGSSG NASEVSVACL TERIHQMEEN QHSTAEELQA TLQELADLQQ ITQELNGENE
RLGEEKVILM DSLCQQSDKL ELYGRQIEYL RSLLDEHHVS YVLEEDIKSG RYMELEQRYA
DLAENGRFER EQLLGVQQHL SNTLKMAEQD NAEAQEMIGA LKERNHQMER IMESERQGRA
AVEATLEEYK EVASSDQAEL SRCRAQLEQE RQRVAELYSL HTAGDKNDIC QLLEGVRLGK
EEAEAKAAKL QEGLEQAHGE LSHLRETFSK LDREYREFQE QAQQQMGEQE RALEKQRLDL
QEKETEVADM KETIFELEDE VEQHRALKLH DNLIITDLEN SVKKLQDQKH DMEREIKILH
RRLREESMEW RQFQADLQTA VVIANDIKSE AQEEIGDLRR RLQEAQEKNE KLSKELEEVK
SRKQDEERGR VYNYMNAVER DLAALRQGMG LSRRSSTSSE PSPTVKTLIK SFDSASQGPP
SSGASVTPTA SAAPLPRTPL SPSPMKTPPA AAVSPIQRHS VSGSMSAAKP LSSLGDKRPT
YPDISLPAEH LLRGSAAGRP PSALQRVSNM DSTKAISVSR RSSEEMKRDM AAPDGASSAS
LMAMSAASSP LALASSSPTA SVTPTTRSRL REERKDPLSA LAREYGGSKR NALLKWCQKK
TEGYQNIDIT NFSSSWNDGL AFCAVLHTYL PAHIPYQELT SQEKRRNFTL AFQAAESVGI
KCTLDINEMV HTERPDWQSV MTYVTAIYKY FET
