SLAI2_BOVIN
ID SLAI2_BOVIN Reviewed; 582 AA.
AC Q3MHV6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=SLAIN motif-containing protein 2;
GN Name=SLAIN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Promotes cytoplasmic
CC microtubule nucleation and elongation. Required for normal structure of
CC the microtubule cytoskeleton during interphase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Colocalizes with microtubules. Detected at the plus end of growing
CC microtubules (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminus forms a two-stranded coiled coil. {ECO:0000250}.
CC -!- PTM: Is highly phosphorylated during mitosis, but not during
CC interphase. The highly phosphorylated form does not localize at
CC microtubule plus ends and does not interact with MAPRE1 or CKAP5 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC {ECO:0000305}.
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DR EMBL; BC104624; AAI04625.1; -; mRNA.
DR RefSeq; NP_001030482.1; NM_001035405.1.
DR AlphaFoldDB; Q3MHV6; -.
DR SMR; Q3MHV6; -.
DR STRING; 9913.ENSBTAP00000029282; -.
DR PaxDb; Q3MHV6; -.
DR PRIDE; Q3MHV6; -.
DR Ensembl; ENSBTAT00000079432; ENSBTAP00000067474; ENSBTAG00000021963.
DR GeneID; 534203; -.
DR KEGG; bta:534203; -.
DR CTD; 57606; -.
DR VEuPathDB; HostDB:ENSBTAG00000021963; -.
DR VGNC; VGNC:34652; SLAIN2.
DR eggNOG; ENOG502QSZP; Eukaryota.
DR GeneTree; ENSGT00390000017860; -.
DR HOGENOM; CLU_027278_2_0_1; -.
DR InParanoid; Q3MHV6; -.
DR OrthoDB; 616171at2759; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000021963; Expressed in cardiac ventricle and 106 other tissues.
DR ExpressionAtlas; Q3MHV6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR InterPro; IPR026179; Slain.
DR PANTHER; PTHR22406; PTHR22406; 1.
DR Pfam; PF15301; SLAIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..582
FT /note="SLAIN motif-containing protein 2"
FT /id="PRO_0000316966"
FT REGION 28..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..39
FT /evidence="ECO:0000255"
FT COMPBIAS 200..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 582
FT /note="Important for interaction with CLIP1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 539
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT MOD_RES 552
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
SQ SEQUENCE 582 AA; 62770 MW; D8C00D475ABEC83D CRC64;
MEDVNSDVNA DQEVRKLQEL VKMLEKQNEQ LRSRSGAVQG AGSFGPGSPV RAGASTPSSG
TASPRGFPLG LSAKSGSGAG SGPRRTSSEE LRDATSLLAA GEGGLLDEVE PLRPEELERL
SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA
LKRQNLYNNP FNSVSYTSPY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS
SDRNPPLSPQ SSIDSELSAS ELDEDSIGSN YKLNDVTDVQ ILARMQEESL RQEYAATASR
RSSGSSCNST RRGTFSDQEL DAQSLDDEDD NMHHAVYPAV NRFSPSPRNS PRPSPKQSPR
NSPRSRSPAR GIEYSRVSPQ PMISRLQQPR LSLQGHPTDL QTTNVKNEEK LRRSLPNLSR
TSNTQVDSVK SSRSDSNFQV PNGGIPRMQP QASAIPSPGK FRSPAAPSPL ALRQPVKAFS
NHGSGSPGSQ ETTQLMQTTS SPGPPMVQNT VPANPPSNIN STTLTRPAGT TVMRSGLPRP
SAPSAGGIPV PRSKLAQPVR RSLPAPKTYG SMKDDSWKDG CY
