Q922J3

SS
Gene name
Clip1 (Kiaa4046, Rsn)
Protein name
CAP-Gly domain-containing linker protein 1
Names
Cytoplasmic linker protein 170, CLIP-170, Restin
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:56430
EC number
Protein Class

Descriptions

Cytoplasmic linker protein (CLIP-170 or CLIP1) is a prototype of the plus end-tracking proteins that regulate microtubule dynamics. The CAP-Gly-2 domain possesses a basic groove and directly binds the EExEEY/F motif of the C-terminal acidic-tail ends of α-tubulin. The C-terminal zinc knuckle domains of CLIP-170 bind the basic groove to inhibit the binding to the acidic tails. Once CLIP-170 binds microtubule, the released zinc knuckle domain may serve to recruit dynein to the plus end by interacting with the dynactin subunit p150Glued and LIS1.

Autoinhibitory domains (AIDs)

1370-1387 (C-terminal zinc knuckle domains) SS

Target domain

213-278 (CAP-Gly-2 domain)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for Q922J3

Entry ID Method Resolution Chain Position Source
2CP7 NMR - A 58-128 PDB
AF-Q922J3-F1 Predicted AlphaFoldDB

10 variants for Q922J3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs245757834 50 T>I No Ensembl
rs37960430 228 R>C No Ensembl
rs240677501 476 A>V No Ensembl
rs245492188 602 I>V No Ensembl
rs37875732 666 V>I No Ensembl
rs242323999 710 E>K No Ensembl
rs29529702 738 E>K No Ensembl
rs36902261 744 E>K No Ensembl
rs214231814 807 Q>H No Ensembl
rs50592074 1133 V>I No Ensembl

No associated diseases with Q922J3

4 regional properties for Q922J3

Type Name Position InterPro Accession
domain CAP Gly-rich domain 60 - 125 IPR000938-1
domain CAP Gly-rich domain 213 - 278 IPR000938-2
domain CLIP1, zinc knuckle 1329 - 1346 IPR032108-1
domain CLIP1, zinc knuckle 1369 - 1385 IPR032108-2

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell projection, ruffle
  • Localizes to microtubule plus ends
  • Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346)
  • Accumulates in plasma membrane regions with ruffling and protrusions
  • Associates with the membranes of intermediate macropinocytic vesicles (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic microtubule Any microtubule in the cytoplasm of a cell.
cytoplasmic vesicle membrane The lipid bilayer surrounding a cytoplasmic vesicle.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
microtubule cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
microtubule plus-end The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.

5 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
microtubule plus-end binding Binding to the plus end of a microtubule.
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.
zinc ion binding Binding to a zinc ion (Zn).

5 GO annotations of biological process

Name Definition
cytoplasmic microtubule organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins in the cytoplasm of a cell.
microtubule bundle formation A process that results in a parallel arrangement of microtubules.
positive regulation of dendrite development Any process that activates or increases the frequency, rate or extent of dendrite development.
positive regulation of microtubule polymerization Any process that activates or increases the frequency, rate or extent of microtubule polymerization.
protein transport into plasma membrane raft The directed movement of a protein into a plasma membrane raft.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O42184 CLIP1 CAP-Gly domain-containing linker protein 1 Gallus gallus (Chicken) SS
Q9VJE5 CLIP-190 Restin homolog Drosophila melanogaster (Fruit fly) SS
P30622 CLIP1 CAP-Gly domain-containing linker protein 1 Homo sapiens (Human) EV
Q9JK25 Clip1 CAP-Gly domain-containing linker protein 1 Rattus norvegicus (Rat) EV
10 20 30 40 50 60
MSMLKPSGLK APTKILKPGS TALKTPAAAA APVEKTIPSE KASGPPSSET QEEFVDDFRV
70 80 90 100 110 120
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
130 140 150 160 170 180
PSKLTRKVQA EDEANGLQAA PGRTASPLST AAATMVSSSP ATPSNIPHKP SQSTAKEPSA
190 200 210 220 230 240
TPQISNLTKT ASESISNLSE AGSVKKGERE LKVGDRVLVG GTKAGVVRFL GETDFAKGEW
250 260 270 280 290 300
CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
310 320 330 340 350 360
ATPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
370 380 390 400 410 420
QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD
430 440 450 460 470 480
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLEVATVS EKSRIMELEK DLALRAQEVA
490 500 510 520 530 540
ELRRRLESSK PPGDVDMSLS LLQEISALQE KLEAIHTDHQ GEMTSLKEHF GAREEAFQKE
550 560 570 580 590 600
IKALHTATEK LSKENESLRS KLDHANKENS DVIALWKSKL ETAIASHQQA MEELKVSFSK
610 620 630 640 650 660
GIGTDSAEFA ELKTQIERLR LDYQHEIESL QSKQDSERSA HAKEMETMQA KLMKIIKEKE
670 680 690 700 710 720
DSLEAVKARL DSAEDQHLVE MEDTLNKLQE AEIKVKELEV LQAKYTEQSE VIGNFTSQLS
730 740 750 760 770 780
AVKEKLLDLD ALRKANSEGK LELETLRQQL EGAEKQIKNL ETERNAESSK ANSITKELQE
790 800 810 820 830 840
KELVLTGLQD SLNQVNQVKE TLEKELQTLK EKFASTSEEA VSAQTRMQDT VNKLHQKEEQ
850 860 870 880 890 900
FNVLSSELEK LRENLTDMEA KFKEKDDRED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM
910 920 930 940 950 960
NDELRLKERS VEELQLKLTK ANENASFLQK SIGEVTLKAE QSQQQAARKH EEEKKELEEK
970 980 990 1000 1010 1020
LLELEKKMET SYNQCQDLKA KYEKASSETK TKHEEILQNL QKMLADTEDK LKAAQEANRD
1030 1040 1050 1060 1070 1080
LMQDMEELKT QADKAKAAQT AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA RLQNELDTLK
1090 1100 1110 1120 1130 1140
ENNLKTVEEL NKSKELLSVE NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG
1150 1160 1170 1180 1190 1200
RTRDEVTSHQ KLEEERSVLN NQLLEMKKRE SEFRKDADEE KASLQKSISL TSALLTEKDA
1210 1220 1230 1240 1250 1260
ELEKLRNEVT VLRGENATAK SLHSVVQTLE SDKVKLELKV KNLELQLKEN KRQLSSSSGN
1270 1280 1290 1300 1310 1320
TDAQAEEDER AQESQIDFLN SVIVDLQRKN QDLKMKVEMM SEAALNGNGE DLNSYDSDDQ
1330 1340 1350 1360 1370 1380
EKQSKKKPRL FCDICDCFDL HDTEDCPTQA QMSEDPPHST HHGSRSEERP YCEICEMFGH
1390
WATNCNDDET F