Q7ZV15

SS
Gene name
sec22ba (sec22l1a, zgc:56278)
Protein name
Vesicle-trafficking protein SEC22b-A
Names
SEC22 vesicle-trafficking protein homolog B-A
Species
Mus musculus (Mouse)
KEGG Pathway
dre:114464
EC number
Protein Class

Descriptions

Von Willebrand Factor (VWF) is a giant extracellular protein playing a key role in blood clotting. Activated by shear-stress, VWF crosslinks the endothelial extracellular matrix with blood platelets at the site of vascular injury. Functional VWF is a linear multimer of tens of covalently linked monomers, extending up to 15 mm. Autoinhibition of VWF is mediated by the A1-A2 domain-domain interaction. The VWF A2 domain targets and blocks specific regions of the VWF A1 domain that correspond to the binding site of the platelet glycoprotein Iba (GPIba) receptor. A stretching force unblocks the GPIba binding site by dissociating the A1A2 complex. Also, the autoinhibitory modules (AIMs) flanking the VWF-A1 domain contribute to autoinhibition of the VWF. The N-terminal AIM cooperates with the C-terminal AIM to form a joint Rotini-like structure, partially autoinhibiting the VWF-A1-GPIba interaction.

Autoinhibitory domains (AIDs)

1-119 (Longin domain) SS

Target domain

134-194 (v-SNARE coiled-coil homology)

Relief mechanism

Others, PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q7ZV15

Entry ID Method Resolution Chain Position Source
AF-Q7ZV15-F1 Predicted AlphaFoldDB

No variants for Q7ZV15

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7ZV15

No associated diseases with Q7ZV15

3 regional properties for Q7ZV15

Type Name Position InterPro Accession
binding_site IQ motif, EF-hand binding site 159 - 181 IPR000048-1
binding_site IQ motif, EF-hand binding site 205 - 235 IPR000048-2
domain ATPase, AAA-type, core 563 - 680 IPR003959

Functions

Description
EC Number
Subcellular Localization
  • Secreted
  • Secreted, extracellular space, extracellular matrix
  • Localized to storage granules
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
endoplasmic reticulum-Golgi intermediate compartment A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
endoplasmic reticulum-Golgi intermediate compartment membrane The lipid bilayer surrounding any of the compartments of the endoplasmic reticulum (ER)-Golgi intermediate compartment system.
ER to Golgi transport vesicle membrane The lipid bilayer surrounding a vesicle transporting substances from the endoplasmic reticulum to the Golgi.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
melanosome A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells.
SNARE complex A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.

1 GO annotations of molecular function

Name Definition
SNAP receptor activity Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.

4 GO annotations of biological process

Name Definition
endoplasmic reticulum to Golgi vesicle-mediated transport The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
vesicle fusion with Golgi apparatus The joining of the lipid bilayer membrane around a vesicle to the lipid bilayer membrane around the Golgi.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZJW4 SEC22B Vesicle-trafficking protein SEC22b Gallus gallus (Chicken) SS
O75396 SEC22B Vesicle-trafficking protein SEC22b Homo sapiens (Human) SS
O08547 Sec22b Vesicle-trafficking protein SEC22b Mus musculus (Mouse) EV
Q4KM74 Sec22b Vesicle-trafficking protein SEC22b Rattus norvegicus (Rat) SS
Q94AU2 SEC22 25.3 kDa vesicle transport protein Arabidopsis thaliana (Mouse-ear cress) PR
Q6P7L4 sec22b Vesicle-trafficking protein SEC22b Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
Q7SXP0 sec22bb Vesicle-trafficking protein SEC22b-B Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MNPFRYEICL LVLALTWPGT LCTEKPRDRP STARCSLFGD DFINTFDETM YSFAGGCSYL
70 80 90 100 110 120
LAGDCQKRSF SILGNFQDGK RMSLSVYLGE FFDIHLFANG TVMQGDQSIS MPYASQGLYL
130 140 150 160 170 180
ELEAGYYKLS SETFGFAARI DGNGNFQVLM SDRHFNKTCG LCGDFNIFAE DDFRTQEGTL
190 200 210 220 230 240
TSDPYDFANS WALSSEEQRC KRASPPSRNC ESSSGDMHQA MWEQCQLLKT ASVFARCHPL
250 260 270 280 290 300
VDPESFVALC EKILCTCATG PECACPVLLE YARTCAQEGM VLYGWTDHSA CRPACPAGME
310 320 330 340 350 360
YKECVSPCPR TCQSLSINEV CQQQCVDGCS CPEGELLDED RCVQSSDCPC VHAGKRYPPG
370 380 390 400 410 420
TSLSQDCNTC ICRNSLWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCED
430 440 450 460 470 480
HTFSIVIETM QCADDPDAVC TRSVSVRLSA LHNSLVKLKH GGAVGIDGQD VQLPFLQGDL
490 500 510 520 530 540
RIQHTVMASV RLSYAEDLQM DWDGRGRLLV KLSPVYSGKT CGLCGNYNGN KGDDFLTPAG
550 560 570 580 590 600
LVEPLVVDFG NAWKLQGDCS DLRRQHSDPC SLNPRLTRFA EEACALLTSS KFEACHHAVS
610 620 630 640 650 660
PLPYLQNCRY DVCSCSDSRD CLCNAVANYA AECARKGVHI GWREPGFCAL GCPQGQVYLQ
670 680 690 700 710 720
CGNSCNLTCR SLSLPDEECS EVCLEGCYCP PGLYQDERGD CVPKAQCPCY YDGELFQPAD
730 740 750 760 770 780
IFSDHHTMCY CEDGFMHCTT SGTLGSLLPD TVLSSPLSHR SKRSLSCRPP MVKLVCPADN
790 800 810 820 830 840
PRAQGLECAK TCQNYDLERM SLGCVSGCLC PPGMVRHENK CVALERCPCF HQGAEYAPGD
850 860 870 880 890 900
TVKIGCNTCV CRERKWNCTN HVCDATRSAI GMAHYLTFDG LKYLFPGECQ YVLVYDYCGS
910 920 930 940 950 960
NPGTFQILVG NEGCSYPSVK CRKRVTILVD GGELELFDGE VNVKRPLRDE SHFEVVESGR
970 980 990 1000 1010 1020
YVILLLGQAL SVVWDHHLSI SVVLKHTYQE QVCGLCGNFD GIQNNDSTTS SLQVEEDPVN
1030 1040 1050 1060 1070 1080
FGNSWKVSSQ CADTRKLSLD VSPATCHNNI MKQTMVDSAC RILTSDVFQG CNRLVDPEPY
1090 1100 1110 1120 1130 1140
LDICIYDTCS CESIGDCACF CDTIAAYAHV CAQHGQVVAW RTPTLCPQSC EEKNVRENGY
1150 1160 1170 1180 1190 1200
ECEWRYNSCA PACPVTCQHP EPLACPVQCV EGCHAHCPPG RILDELLQTC VDPQDCPVCE
1210 1220 1230 1240 1250 1260
VAGRRLAPGK KITLSPDDPA HCQNCHCDGV NLTCEACQEP GGLVAPPTDA PVSSTTPYVE
1270 1280 1290 1300 1310 1320
DTPEPPLHNF YCSKLLDLVF LLDGSSMLSE AEFEVLKAFV VGMMERLHIS QKRIRVAVVE
1330 1340 1350 1360 1370 1380
YHDGSRAYLE LKARKRPSEL RRITSQIKYT GSQVASTSEV LKYTLFQIFG KIDRPEASHI
1390 1400 1410 1420 1430 1440
TLLLTASQEP PRMARNLVRY VQGLKKKKVI VIPVGIGPHA SLKQIRLIEK QAPENKAFLL
1450 1460 1470 1480 1490 1500
SGVDELEQRR DEIVSYLCDL APEAPAPTQP PQVAHVTVSP GIAGISSPGP KRKSMVLDVV
1510 1520 1530 1540 1550 1560
FVLEGSDEVG EANFNKSKEF VEEVIQRMDV SPDATRISVL QYSYTVTMEY AFNGAQSKEE
1570 1580 1590 1600 1610 1620
VLRHVREIRY QGGNRTNTGQ ALQYLSEHSF SPSQGDRVEA PNLVYMVTGN PASDEIKRLP
1630 1640 1650 1660 1670 1680
GDIQVVPIGV GPHANMQELE RISRPIAPIF IRDFETLPRE APDLVLQTCC SKEGLQLPTL
1690 1700 1710 1720 1730 1740
PPLPDCSQPL DVVLLLDGSS SLPESSFDKM KSFAKAFISK ANIGPHLTQV SVIQYGSINT
1750 1760 1770 1780 1790 1800
IDVPWNVVQE KAHLQSLVDL MQQEGGPSQI GDALAFAVRY VTSQIHGARP GASKAVVIII
1810 1820 1830 1840 1850 1860
MDTSLDPVDT AADAARSNRV AVFPVGVGDR YDEAQLRILA GPGASSNVVK LQQVEDLSTM
1870 1880 1890 1900 1910 1920
ATLGNSFFHK LCSGFSGVCV DEDGNEKRPG DVWTLPDQCH TVTCLANGQT LLQSHRVNCD
1930 1940 1950 1960 1970 1980
HGPRPSCANS QSPVRVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVIFQNK
1990 2000 2010 2020 2030 2040
EQDLEVLLHN GACSPGAKQA CMKSIEIKHA GVSAELHSNM EMAVDGRLVL APYVGENMEV
2050 2060 2070 2080 2090 2100
SIYGAIMYEV RFTHLGHILT YTPQNNEFQL QLSPKTFASK MHGLCGICDE NGANDFTLRD
2110 2120 2130 2140 2150 2160
GTVTTDWKRL VQEWTVQQPG YTCQAVPEEQ CPVSDSSHCQ VLLSASFAEC HKVIAPATFH
2170 2180 2190 2200 2210 2220
TICQQDSCHQ ERVCEVIASY AHLCRTSGVC VDWRTTDFCA MSCPPSLVYN HCERGCPRHC
2230 2240 2250 2260 2270 2280
DGNTSFCGDH PSEGCFCPQH QVFLEGSCVP EEACTQCVGE DGVRHQFLET WVPDHQPCQI
2290 2300 2310 2320 2330 2340
CMCLSGRKIN CTAQPCPTAR APTCGPCEVA RLKQSTNLCC PEYECVCDLF NCNLPPVPPC
2350 2360 2370 2380 2390 2400
EGGLQPTLTN PGECRPTFTC DCRKEECKRV SPPSCPPHRT PTLRKTQCCD EYECACSCVN
2410 2420 2430 2440 2450 2460
STLSCPLGYL ASATTNDCGC TTTTCLPDKV CVHRGTVYPV GQFWEEGCDT CTCTDMEDTV
2470 2480 2490 2500 2510 2520
VGLRVVQCSQ RPCEDSCQPG FSYVLHEGEC CGRCLPSACK VVAGSLRGDS HSSWKSVGSR
2530 2540 2550 2560 2570 2580
WAVPENPCLV NECVRVEDAV FVQQRNISCP QLAVPTCPTG FQLNCETSEC CPSCHCEPVE
2590 2600 2610 2620 2630 2640
ACLLNGTIIG PGKSVMVDLC TTCRCIVQTD AISRFKLECR KTTCEACPMG YREEKSQGEC
2650 2660 2670 2680 2690 2700
CGRCLPTACT IQLRGGRIMT LKQDETFQDG CDSHLCRVNE RGEYIWEKRV TGCPPFDEHK
2710 2720 2730 2740 2750 2760
CLAEGGKIVK IPGTCCDTCE EPDCKDITAK VQYIKVGDCK SQEEVDIHYC QGKCASKAVY
2770 2780 2790 2800 2810
SIDIEDVQEQ CSCCLPSRTE PMRVPLHCTN GSVVYHEVIN AMQCRCSPRN CSK